Przewidywanie ciężkości COVID-19 za pomocą swoistego
Związek między poziomami alarmin w surowicy a wskaźnikami określanymi dla chorób u pacjentów z zapaleniem przeciwciał związanym z cytoplazmatycznymi przeciwciałami przeciw neutrofilom
Wstęp / cel: Oceniliśmy związek między stężeniem alarmyny w surowicy a wskaźnikami specyficznymi dla choroby u pacjentów z zapaleniem naczyń związanym z przeciwciałami antyneutrofilowymi (ANCA ).
Pacjenci i metody: Wykorzystano surowice i dane od 79 pacjentów. W przypadku wskaźników specyficznych dla AAV zebrano wynik aktywności zapalenia naczyń Birmingham (BVAS), punktację pięcioczynnikową (FFS) i wskaźnik uszkodzenia zapalenia naczyń (VDI) oraz poziomy czterech alarmin w surowicy (czynnik wzrostu pochodzenia wątrobiaka, białko skrzynki 1 grupy o wysokiej mobilności , S100A9 i S100A12) mierzono za pomocą enzymatycznego testu immunosorpcyjnego. Oceniono związki między poziomami alarmin, wskaźnikami swoistymi dla AAV i laboratoryjnymi markerami stanu zapalnego.
Wyniki: Poziomy S100A9 były istotnie skorelowane z poziomem białka C-reaktywnego (r = 0,316, p = 0,005), a poziomy S100A12 korelowały z VDI (r = 0,232, p = 0,040), co było zgodne w podgrupie pacjentów z mieloperoksydazą (okołojądrowe ) -ANCA pozytywność. Nie znaleziono innych powiązań między poziomami alarmin a BVAS , FFS i VDI.
Wniosek: Stężenie S100A12 w surowicy było związane z uszkodzeniem narządów w AAV, zwłaszcza u pacjentów z dodatnim wynikiem badania mieloperoksydazy (okołojądrowej) -ANCA .
Zapalenie skórno-mięśniowe z dodatnim przeciwciałem anty-MDA5 z szybko postępującą śródmiąższową chorobą płuc: opis „Obstawianie”
Przeciwciało dodatnie w zapaleniu skórno – mięśniowym (DM) białku 5 związanym z różnicowaniem czerniaka (MDA5 ) wykazuje wyjątkowe cechy skórne i patologiczne. Opisujemy dwa przypadki szybko postępującej śródmiąższowej choroby płuc związanej z zapaleniem mięśni (RP-ILD).
Pacjentkami były dwie kobiety z Kerali w Indiach. Obaj pacjenci mieli zapalenie mięśni z dodatnim wynikiem oznaczenia przeciwciał anty-MDA5. Obaj pacjenci zgłosili się z RP-ILD bez klinicznych cech zapalenia mięśni i ulegli chorobie pomimo agresywnego leczenia. DM z dodatnim przeciwciałem przeciw MDA5 charakteryzuje się chorobą amiopatyczną z szybko postępującą i śmiertelną ILD.
Description: IGF-BPs control the distribution, function and activity of IGFs in various cell tissues and body fluids. IGF-BP4 is the major IGF-BP produced by osteoblasts, and is also found in the epidermis, ovarian follicles, and other tissues. IGF-BP4 inhibits the activity of IGF-I and IGF-II by binding in a manner that results in the formation of complexes with reduced ability to signal through cell surface IGF receptors. IGF-BP4 can inhibit the growth of chick pelvis cartilage and HT29 colon adenocarcinoma cells by blocking the mitogenic actions of IGFs, and has also been shown to reduce colony formation by colorectal cancer cells via an IGF independent pathway. The biological effects of IGF-BP4 can be regulated by Pregnancy Associated Plasma Protein A (PAPP-A), which reduces IGF-BP4/IGF binding affinity by proteolytically cleaving IGF-BP4. The modulation of IGF-BP4 activity by PAPP-A is an important component in the regulation of ovarian folliculogenesis and in the growth inhibition of responding ovarian cancer cells. Recombinant human IGF-BP4 is a 26.1 kDa protein consisting of 238 amino acid residues including the IGF-BP domain and thyroglobulin type-I domain.
Description: IGF-BPs control the distribution, function and activity of IGFs in various cell tissues and body fluids. IGF-BP4 is the major IGF-BP produced by osteoblasts, and is also found in the epidermis, ovarian follicles, and other tissues. IGF-BP4 inhibits the activity of IGF-I and IGF-II by binding in a manner that results in the formation of complexes with reduced ability to signal through cell surface IGF receptors. IGF-BP4 can inhibit the growth of chick pelvis cartilage and HT29 colon adenocarcinoma cells by blocking the mitogenic actions of IGFs, and has also been shown to reduce colony formation by colorectal cancer cells via an IGF independent pathway. The biological effects of IGF-BP4 can be regulated by Pregnancy Associated Plasma Protein A (PAPP-A), which reduces IGF-BP4/IGF binding affinity by proteolytically cleaving IGF-BP4. The modulation of IGF-BP4 activity by PAPP-A is an important component in the regulation of ovarian folliculogenesis and in the growth inhibition of responding ovarian cancer cells. Recombinant human IGF-BP4 is a 26.1 kDa protein consisting of 238 amino acid residues including the IGF-BP domain and thyroglobulin type-I domain.
Description: IGF-BPs control the distribution, function and activity of IGFs in various cell tissues and body fluids. IGF-BP4 is the major IGF-BP produced by osteoblasts, and is also found in the epidermis, ovarian follicles, and other tissues. IGF-BP4 inhibits the activity of IGF-I and IGF-II by binding in a manner that results in the formation of complexes with reduced ability to signal through cell surface IGF receptors. IGF-BP4 can inhibit the growth of chick pelvis cartilage and HT29 colon adenocarcinoma cells by blocking the mitogenic actions of IGFs, and has also been shown to reduce colony formation by colorectal cancer cells via an IGF independent pathway. The biological effects of IGF-BP4 can be regulated by Pregnancy Associated Plasma Protein A (PAPP-A), which reduces IGF-BP4/IGF binding affinity by proteolytically cleaving IGF-BP4. The modulation of IGF-BP4 activity by PAPP-A is an important component in the regulation of ovarian folliculogenesis and in the growth inhibition of responding ovarian cancer cells. Recombinant human IGF-BP4 is a 25.8 kDa protein consisting of 237 amino acid residues including the IGF-BP domain and thyroglobulin type-I domain.
*Manufactured using (BTI-Tn-5B1-4) cells under license from the Boyce Thompson Institute for Plant Research, Inc.
Description: IGF-BPs control the distribution, function and activity of IGFs in various cell tissues and body fluids. IGF-BP4 is the major IGF-BP produced by osteoblasts, and is also found in the epidermis, ovarian follicles, and other tissues. IGF-BP4 inhibits the activity of IGF-I and IGF-II by binding in a manner that results in the formation of complexes with reduced ability to signal through cell surface IGF receptors. IGF-BP4 can inhibit the growth of chick pelvis cartilage and HT29 colon adenocarcinoma cells by blocking the mitogenic actions of IGFs, and has also been shown to reduce colony formation by colorectal cancer cells via an IGF independent pathway. The biological effects of IGF-BP4 can be regulated by Pregnancy Associated Plasma Protein A (PAPP-A), which reduces IGF-BP4/IGF binding affinity by proteolytically cleaving IGF-BP4. The modulation of IGF-BP4 activity by PAPP-A is an important component in the regulation of ovarian folliculogenesis and in the growth inhibition of responding ovarian cancer cells. Recombinant human IGF-BP4 is a 25.8 kDa protein consisting of 237 amino acid residues including the IGF-BP domain and thyroglobulin type-I domain.
Description: IGF-BPs control the distribution, function and activity of IGFs in various cell tissues and body fluids. IGF-BP4 is the major IGF-BP produced by osteoblasts, and is also found in the epidermis, ovarian follicles, and other tissues. IGF-BP4 inhibits the activity of IGF-I and IGF-II by binding in a manner that results in the formation of complexes with reduced ability to signal through cell surface IGF receptors. IGF-BP4 can inhibit the growth of chick pelvis cartilage and HT29 colon adenocarcinoma cells by blocking the mitogenic actions of IGFs, and has also been shown to reduce colony formation by colorectal cancer cells via an IGF independent pathway. The biological effects of IGF-BP4 can be regulated by Pregnancy Associated Plasma Protein A (PAPP-A), which reduces IGF-BP4/IGF binding affinity by proteolytically cleaving IGF-BP4. The modulation of IGF-BP4 activity by PAPP-A is an important component in the regulation of ovarian folliculogenesis and in the growth inhibition of responding ovarian cancer cells. Recombinant human IGF-BP4 is a 25.8 kDa protein consisting of 237 amino acid residues including the IGF-BP domain and thyroglobulin type-I domain.
Description: The superfamily of insulin-like growth factor (IGF) binding proteins include the six high-affinity IGF binding proteins (IGFBP) and several low-affinity binding proteins referred to as IGFBP related proteins (IGFBP-rP). All IGFBP superfamily members are cysteine-rich proteins with conserved cysteine residues, which are clustered in the amino- and carboxy-terminal thirds of the molecule. IGFBPs modulate the biological activities of IGF proteins. Some IGFBPs may also have intrinsic bioactivity that is independent of their ability to bind IGF proteins. Post-translational modifications of IGFBP, including glycosylation, phosphorylation and proteolysis, have been shown to modify the affinities of the binding proteins to IGF.
Description: The superfamily of insulin-like growth factor (IGF) binding proteins include the six high-affinity IGF binding proteins (IGFBP) and several low-affinity binding proteins referred to as IGFBP related proteins (IGFBP-rP). All IGFBP superfamily members are cysteine-rich proteins with conserved cysteine residues, which are clustered in the amino- and carboxy-terminal thirds of the molecule. IGFBPs modulate the biological activities of IGF proteins. Some IGFBPs may also have intrinsic bioactivity that is independent of their ability to bind IGF proteins. Post-translational modifications of IGFBP, including glycosylation, phosphorylation and proteolysis, have been shown to modify the affinities of the binding proteins to IGF.
Description: The superfamily of insulin-like growth factor (IGF) binding proteins include the six high-affinity IGF binding proteins (IGFBP) and several low-affinity binding proteins referred to as IGFBP related proteins (IGFBP-rP). All IGFBP superfamily members are cysteine-rich proteins with conserved cysteine residues, which are clustered in the amino- and carboxy-terminal thirds of the molecule. IGFBPs modulate the biological activities of IGF proteins. Some IGFBPs may also have intrinsic bioactivity that is independent of their ability to bind IGF proteins. Post-translational modifications of IGFBP, including glycosylation, phosphorylation and proteolysis, have been shown to modify the affinities of the binding proteins to IGF.
Description: The superfamily of insulin-like growth factor (IGF) binding proteins include the six high-affinity IGF binding proteins (IGFBP) and several low-affinity binding proteins referred to as IGFBP related proteins (IGFBP-rP). All IGFBP superfamily members are cysteine-rich proteins with conserved cysteine residues, which are clustered in the amino- and carboxy-terminal thirds of the molecule. IGFBPs modulate the biological activities of IGF proteins. Some IGFBPs may also have intrinsic bioactivity that is independent of their ability to bind IGF proteins. Post-translational modifications of IGFBP, including glycosylation, phosphorylation and proteolysis, have been shown to modify the affinities of the binding proteins to IGF.
Description: The superfamily of insulin-like growth factor (IGF) binding proteins include the six high-affinity IGF binding proteins (IGFBP) and several low-affinity binding proteins referred to as IGFBP related proteins (IGFBP-rP). All IGFBP superfamily members are cysteine-rich proteins with conserved cysteine residues, which are clustered in the amino- and carboxy-terminal thirds of the molecule. IGFBPs modulate the biological activities of IGF proteins. Some IGFBPs may also have intrinsic bioactivity that is independent of their ability to bind IGF proteins. Post-translational modifications of IGFBP, including glycosylation, phosphorylation and proteolysis, have been shown to modify the affinities of the binding proteins to IGF.
Description: The superfamily of insulin-like growth factor (IGF) binding proteins include the six high-affinity IGF binding proteins (IGFBP) and several low-affinity binding proteins referred to as IGFBP related proteins (IGFBP-rP). All IGFBP superfamily members are cysteine-rich proteins with conserved cysteine residues, which are clustered in the amino- and carboxy-terminal thirds of the molecule. IGFBPs modulate the biological activities of IGF proteins. Some IGFBPs may also have intrinsic bioactivity that is independent of their ability to bind IGF proteins. Post-translational modifications of IGFBP, including glycosylation, phosphorylation and proteolysis, have been shown to modify the affinities of the binding proteins to IGF.
Description: The superfamily of insulin-like growth factor (IGF) binding proteins include the six high-affinity IGF binding proteins (IGFBP) and several low-affinity binding proteins referred to as IGFBP related proteins (IGFBP-rP). All IGFBP superfamily members are cysteine-rich proteins with conserved cysteine residues, which are clustered in the amino- and carboxy-terminal thirds of the molecule. IGFBPs modulate the biological activities of IGF proteins. Some IGFBPs may also have intrinsic bioactivity that is independent of their ability to bind IGF proteins. Post-translational modifications of IGFBP, including glycosylation, phosphorylation and proteolysis, have been shown to modify the affinities of the binding proteins to IGF.
Description: The superfamily of insulin-like growth factor (IGF) binding proteins include the six high-affinity IGF binding proteins (IGFBP) and several low-affinity binding proteins referred to as IGFBP related proteins (IGFBP-rP). All IGFBP superfamily members are cysteine-rich proteins with conserved cysteine residues, which are clustered in the amino- and carboxy-terminal thirds of the molecule. IGFBPs modulate the biological activities of IGF proteins. Some IGFBPs may also have intrinsic bioactivity that is independent of their ability to bind IGF proteins. Post-translational modifications of IGFBP, including glycosylation, phosphorylation and proteolysis, have been shown to modify the affinities of the binding proteins to IGF.
Description: The superfamily of insulin-like growth factor (IGF) binding proteins include the six high-affinity IGF binding proteins (IGFBP) and several low-affinity binding proteins referred to as IGFBP related proteins (IGFBP-rP). All IGFBP superfamily members are cysteine-rich proteins with conserved cysteine residues, which are clustered in the amino- and carboxy-terminal thirds of the molecule. IGFBPs modulate the biological activities of IGF proteins. Some IGFBPs may also have intrinsic bioactivity that is independent of their ability to bind IGF proteins. Post-translational modifications of IGFBP, including glycosylation, phosphorylation and proteolysis, have been shown to modify the affinities of the binding proteins to IGF.
Description: Insulin-like growth factor (IGF)-I (also known as somatomedin C and somatomedin A) and IGF-II (multiplication stimulating activity or MSA) belong to the family of insulin-like growth factors that are structurally homologous to proinsulin. Mature IGF-I and IGF-II share approximately 70% sequence identity. Both IGF-I and IGF-II are expressed in many tissues and cell types and may have autocrine, paracrine and endocrine functions. Mature IGF-I and IGF-II are highly conserved between the human, bovine and porcine proteins (100% identity), and exhibit cross-species activity.
Description: Insulin-like growth factor (IGF)-I (also known as somatomedin C and somatomedin A) and IGF-II (multiplication stimulating activity or MSA) belong to the family of insulin-like growth factors that are structurally homologous to proinsulin. Mature IGF-I and IGF-II share approximately 70% sequence identity. Both IGF-I and IGF-II are expressed in many tissues and cell types and may have autocrine, paracrine and endocrine functions. Mature IGF-I and IGF-II are highly conserved between the human, bovine and porcine proteins (100% identity), and exhibit cross-species activity.
Description: Insulin-like growth factor (IGF)-I (also known as somatomedin C and somatomedin A) and IGF-II (multiplication stimulating activity or MSA) belong to the family of insulin-like growth factors that are structurally homologous to proinsulin. Mature IGF-I and IGF-II share approximately 70% sequence identity. Both IGF-I and IGF-II are expressed in many tissues and cell types and may have autocrine, paracrine and endocrine functions. Mature IGF-I and IGF-II are highly conserved between the human, bovine and porcine proteins (100% identity), and exhibit cross-species activity.
Description: Insulin-like growth factor (IGF)-I (also known as somatomedin C and somatomedin A) and IGF-II (multiplication stimulating activity or MSA) belong to the family of insulin-like growth factors that are structurally homologous to proinsulin. Mature IGF-I and IGF-II share approximately 70% sequence identity. Both IGF-I and IGF-II are expressed in many tissues and cell types and may have autocrine, paracrine and endocrine functions. Mature IGF-I and IGF-II are highly conserved between the human, bovine and porcine proteins (100% identity), and exhibit cross-species activity.
Description: A polyclonal antibody for IGF-1 from Human | Mouse. The antibody is produced in rabbit after immunization with human synthetic peptide from the mid-protein of Human IGF-1. The Antibody is tested and validated for WB, ICC/IF, IHC assays with the following recommended dilutions: WB (1:1000); ICC/IF (1:100); IHC (1:50). This IGF-1 antibody is conjugated to ATTO 565.
Description: A polyclonal antibody for IGF-1 from Human | Mouse. The antibody is produced in rabbit after immunization with human synthetic peptide from the mid-protein of Human IGF-1. The Antibody is tested and validated for WB, ICC/IF, IHC assays with the following recommended dilutions: WB (1:1000); ICC/IF (1:100); IHC (1:50). This IGF-1 antibody is conjugated to ATTO 633.
Description: A polyclonal antibody for IGF-1 from Human | Mouse. The antibody is produced in rabbit after immunization with human synthetic peptide from the mid-protein of Human IGF-1. The Antibody is tested and validated for WB, ICC/IF, IHC assays with the following recommended dilutions: WB (1:1000); ICC/IF (1:100); IHC (1:50). This IGF-1 antibody is conjugated to ATTO 655.
Description: A polyclonal antibody for IGF-1 from Human | Mouse. The antibody is produced in rabbit after immunization with human synthetic peptide from the mid-protein of Human IGF-1. The Antibody is tested and validated for WB, ICC/IF, IHC assays with the following recommended dilutions: WB (1:1000); ICC/IF (1:100); IHC (1:50). This IGF-1 antibody is conjugated to ATTO 680.
Description: A polyclonal antibody for IGF-1 from Human | Mouse. The antibody is produced in rabbit after immunization with human synthetic peptide from the mid-protein of Human IGF-1. The Antibody is tested and validated for WB, ICC/IF, IHC assays with the following recommended dilutions: WB (1:1000); ICC/IF (1:100); IHC (1:50). This IGF-1 antibody is conjugated to ATTO 700.
Description: A polyclonal antibody for IGF-1 from Human | Mouse. The antibody is produced in rabbit after immunization with human synthetic peptide from the mid-protein of Human IGF-1. The Antibody is tested and validated for WB, ICC/IF, IHC assays with the following recommended dilutions: WB (1:1000); ICC/IF (1:100); IHC (1:50). This IGF-1 antibody is conjugated to APC/Cy7.
Description: A polyclonal antibody for IGF-1 from Human | Mouse. The antibody is produced in rabbit after immunization with human synthetic peptide from the mid-protein of Human IGF-1. The Antibody is tested and validated for WB, ICC/IF, IHC assays with the following recommended dilutions: WB (1:1000); ICC/IF (1:100); IHC (1:50). This IGF-1 antibody is conjugated to Dylight 350.
Description: A polyclonal antibody for IGF-1 from Human | Mouse. The antibody is produced in rabbit after immunization with human synthetic peptide from the mid-protein of Human IGF-1. The Antibody is tested and validated for WB, ICC/IF, IHC assays with the following recommended dilutions: WB (1:1000); ICC/IF (1:100); IHC (1:50). This IGF-1 antibody is conjugated to Dylight 405.
Description: A polyclonal antibody for IGF-1 from Human | Mouse. The antibody is produced in rabbit after immunization with human synthetic peptide from the mid-protein of Human IGF-1. The Antibody is tested and validated for WB, ICC/IF, IHC assays with the following recommended dilutions: WB (1:1000); ICC/IF (1:100); IHC (1:50). This IGF-1 antibody is conjugated to Dylight 488.
Description: A polyclonal antibody for IGF-1 from Human | Mouse. The antibody is produced in rabbit after immunization with human synthetic peptide from the mid-protein of Human IGF-1. The Antibody is tested and validated for WB, ICC/IF, IHC assays with the following recommended dilutions: WB (1:1000); ICC/IF (1:100); IHC (1:50). This IGF-1 antibody is conjugated to Dylight 594.
Description: A polyclonal antibody for IGF-1 from Human | Mouse. The antibody is produced in rabbit after immunization with human synthetic peptide from the mid-protein of Human IGF-1. The Antibody is tested and validated for WB, ICC/IF, IHC assays with the following recommended dilutions: WB (1:1000); ICC/IF (1:100); IHC (1:50). This IGF-1 antibody is conjugated to Dylight 633.
Description: A polyclonal antibody for IGF-1 from Human | Mouse. The antibody is produced in rabbit after immunization with human synthetic peptide from the mid-protein of Human IGF-1. The Antibody is tested and validated for WB, ICC/IF, IHC assays with the following recommended dilutions: WB (1:1000); ICC/IF (1:100); IHC (1:50). This IGF-1 antibody is conjugated to PE/ATTO 594.
Description: A polyclonal antibody for IGF-1 from Human | Mouse. The antibody is produced in rabbit after immunization with human synthetic peptide from the mid-protein of Human IGF-1. The Antibody is tested and validated for WB, ICC/IF, IHC assays with the following recommended dilutions: WB (1:1000); ICC/IF (1:100); IHC (1:50). This IGF-1 antibody is conjugated to Streptavidin.
Description: Recombinant Human Cytotoxic T-lymphocyte Protein 4 is produced by our Mammalian expression system and the target gene encoding Lys36-Asp161 is expressed with a Flag tag at the C-terminus.
Przewidywanie ciężkości COVID-19 za pomocą swoistego przeciwciała nukleokapsydowego i poszukiwania ryzyka choroby
Pilnie potrzebne są skuteczne metody przewidywania trajektorii choroby COVID-19. W tym przypadku enzymatyczny take a look at immunosorbentu (ELISA) i analiza mikromacierzy antygenów koronawirusa (COVAM) zmapowały epitopy przeciwciał w osoczu pacjentów z COVID-19 ( n = 86) doświadczających szerokiego zakresu stanów chorobowych. Eksperymenty zidentyfikowały przeciwciała przeciwko 21-resztowemu epitopowi z nukleokapsydu (zwanego Ep9) związanym z ciężką chorobą, w tym przyjęciem na oddział intensywnej opieki medycznej (OIOM), zapotrzebowaniem na respiratory lub śmiercią.
Co ważne, przeciwciała anty-Ep9 można wykryć w ciągu 6 dni od wystąpienia objawów, a czasami w ciągu 1 dnia. Ponadto przeciwciała anty-Ep9 korelują z różnymi chorobami współistniejącymi i cechami nadpobudliwości immunologicznej. Wprowadzamy prostą do obliczenia punktację czynnika ryzyka choroby, aby oszacować ilościowo choroby współistniejące i wiek każdego pacjenta. W przypadku pacjentów z przeciwciałami anty-Ep9 , wyniki powyżej 3,Zero przewidują cięższe wyniki choroby ze współczynnikiem prawdopodobieństwa 13,42 (swoistość 96,7%).
Wyniki położyły podwaliny pod nowy typ prognostyczny COVID-19, umożliwiający wczesną identyfikację i segregację pacjentów wysokiego ryzyka. Takie informacje mogą pomóc w skuteczniejszej interwencji terapeutycznej. ZNACZENIE Pandemia COVID-19 spowodowała ponad dwa miliony zgonów na całym świecie. Pomimo wysiłków w walce z wirusem choroba nadal przytłacza szpitale ciężko chorymi pacjentami.
Diagnozę COVID-19 można łatwo przeprowadzić dzięki wielu niezawodnym platformom testowym; jednak prognozy prognostyczne pozostają nieuchwytne. W tym celu zidentyfikowaliśmy krótki epitop z białka nukleokapsydu SARS-CoV-2, a także ocenę czynnika ryzyka choroby opartą na chorobach współistniejących i wieku. Obecność przeciwciał specyficznie wiążących się z tym epitopem oraz punkt odcięcia może przewidywać ciężkie wyniki COVID-19 ze swoistością 96,7%.
Opis przypadku: autoimmunologiczne zapalenie mózgu z przeciwciałami dekarboksylazy kwasu przeciwglutaminowego: seria „pediatrycznych”
Wstęp: Przeciwciała przeciwko dekarboksylazie kwasu glutaminowego (GAD) są związane z różnymi schorzeniami neurologicznymi opisywanymi u pacjentów, w tym z zespołem sztywnej osoby, ataksją móżdżkową, padaczką oporną na leczenie oraz limbicznym i pozalimbicznym zapaleniem mózgu. Odnotowano kilka opisów przypadków i badań dotyczących zapalenia mózgu związanego z przeciwciałami anty-GAD65 w populacjach dorosłych, ale przypadki pediatryczne są rzadkie. Przeanalizowaliśmy retrospektywnie dane kliniczne trzech pacjentów z dodatnim wynikiem przeciwciał anty-GAD65, aby zbadać różnorodność i cechy kliniczne dziecięcego autoimmunologicznego zapalenia mózgu związanego z przeciwciałami anty-GAD65.
Metody: retrospektywnie przeanalizowano dane kliniczne serii trzech pacjentów z dodatnim wynikiem na obecność przeciwciał anty-GAD65 . Przeciwciała GAD65 oznaczano w surowicy i płynie mózgowo-rdzeniowym przy użyciu testu opartego na komórkach.
Wyniki: Wszyscy trzej pacjenci byli kobietami, a wiek zachorowania wynosił four lata i 9 miesięcy, 6 lat i 16 lat. Ich fenotypy kliniczne obejmowały autoimmunologiczne limbiczne zapalenie mózgu, pozalimbiczne zapalenie mózgu i zapalenie mózgu łączące limbiczne i pozalimbiczne zapalenie mózgu. Objawy kliniczne obejmowały drgawki, deficyty pamięci, senność, dysautonomię i ból głowy. Wszyscy pacjenci mieli nieprawidłowy rezonans magnetyczny i zapis EEG w okolicy karnalnej. Wszyscy pacjenci otrzymali immunoterapię i wykazywali przejściowo dobrą odpowiedź , ale u jednego pacjenta doszło do nawrotu choroby. W trakcie obserwacji jeden pacjent z pozalimbicznym zapaleniem mózgu całkowicie wyzdrowiał, podczas gdy dwóch pacjentów z zajęciem układu limbicznego miało słabe wyniki z oporną na leczenie ogniskową padaczką.
Wniosek: Oprócz limbicznego zapalenia mózgu, pozalimbiczne zapalenie mózgu jest również ważnym fenotypem u pacjentów z dodatnim wynikiem na obecność przeciwciał anty-GAD65. Wczesna diagnoza i immunoterapia mogą złagodzić objawy. Jednak pacjenci z limbicznym zapaleniem mózgu często mają padaczkę oporną na leczenie w fazie przewlekłej i mają złe wyniki odległe.
Charakterystyka przeciwciał monoklonalnych przeciw tężcowi jako pierwszy krok w kierunku badania immunologicznego na produkt szczepionki in vitro
Testy zwalniania serii dla ludzkich i weterynaryjnych szczepionek przeciw tężcowi nadal w dużym stopniu opierają się na metodach z udziałem zwierząt, zwłaszcza w badaniach siły działania. Ilość i jakość antygenu tężcowego obecnego w tych produktach ma ogromne znaczenie dla bezpieczeństwa produktu i efektu klinicznego. Metody immunochemiczne, które mierzą spójność zawartości i jakości antygenu, potencjalnie jako wskaźnik siły działania, mogą być lepszym wyborem i negować potrzebę testu siły in vivo. Te metody immunochemiczne wymagają co najmniej jednego dobrze scharakteryzowanego przeciwciała monoklonalnego (mAb), które jest specyficzne dla docelowego antygenu. W tym artykule przedstawiamy wyniki kompleksowego scharakteryzowania panelu mAb przeciwko tężcowi w celu wybrania przeciwciał, które mogą być użyte doopracowanie testu immunologicznego siły działania in vitro .
Mamy oceniać wiązanie przeciwciała do antygenu (natywnej toksyny), detoksykowany antygen (tężca) zaadsorbowanego antygenu i antygenu ciepła zmienione. Funkcję przeciwciał określono za pomocą wewnętrznego testu neutralizacji opartego na komórkach, aby potwierdzić wcześniejsze dane o sile działania in vivo, które były dostępne dla niektórych, ale nie wszystkich przeciwciał. Ponadto zmierzono powinowactwo przeciwciał i przeprowadzono analizę współzawodnictwa epitopów w celu zidentyfikowania par przeciwciał, które można zastosować w formacie testu immunologicznego kanapkowego. Nie wszystkie testy charakteryzacji dostarczyły dowodów na „wyższość” jednego mAb nad innym, ale łącznie wyniki wszystkich badań charakteryzacji pozwoliły na wybór pary przeciwciał, które miały być wykorzystane do opracowania testu.
Description: Thymus chemokine-1 (TCK-1 or CXCL7)) is a member of the CXC subfamily of chemokines. Mouse TCK-1 shares 72% amino acid sequence identity with rat TCK-1.
Description: NAP-2 or CXCL7 is a CXC chemokine that can signal through the CXCR1 and CXCR2 receptors. It is produced in leukocytes by enzymatic processing of a precursor called platelet basic protein (PBP). NAP-2 chemoattracts and activates neutrophils. Recombinant human NAP-2 protein is a 7.6 kDa protein containing 70 amino acid residues including the four highly conserved cysteine residues present in CXC chemokines, and also including the ELR motif common to CXC chemokines that bind to CXCR1 and CXCR2.
Description: Neutrophil Activating Peptide 2 (NAP2), Connective Tissue Activating Protein III (CTAPIII) and βthrombogulin ( βTG), are proteolytically processed carboxylterminal fragments of platelet basic protein (PBP) which is found in the alphagranules of human platelets. NAP2 is a member of the CXC chemokines. Similar to other ELR domain containing CXC chemokines such as IL8 and the GRO proteins, NAP2 has been shown to bind CXCR2 and to chemoattract and activate neutrophils. Although CTAPIII, βTG and PBP represent aminoterminal extended variants of NAP 2 and possess the same CXC chemokine domains, these proteins do not exhibit NAP2 activity. It has been shown that the additional aminoterminal residues of CTAP III masks the critical ELR receptor binding domain that is exposed on NAP2 and may account for lack of NAP2 activity.
Description: NAP-2 is a CXC chemokine that can signal through the CXCR1 and CXCR2 receptors. It is produced in leukocytes by enzymatic processing of a precursor called platelet basic protein (PBP). NAP-2 chemoattracts and activates neutrophils. Recombinant human NAP-2 protein is a 7-8 kDa protein containing 70 amino acid residues including the four highly conserved cysteine residues present in CXC chemokines, and also including the ELR motif common to CXC chemokines that bind to CXCR1 and CXCR2.
Description: NAP-2 is a CXC chemokine that can signal through the CXCR1 and CXCR2 receptors. It is produced in leukocytes by enzymatic processing of a precursor called platelet basic protein (PBP). NAP-2 chemoattracts and activates neutrophils. Recombinant human NAP-2 protein is a 7-8 kDa protein containing 70 amino acid residues including the four highly conserved cysteine residues present in CXC chemokines, and also including the ELR motif common to CXC chemokines that bind to CXCR1 and CXCR2.
Mouse Platelet Basic Protein / CXCL7 (PPBP) ELISA Kit
Description: A sandwich ELISA kit for quantitative measurement of Mouse ?TG/PBP/CXCL7/NAP2 (Thromboglobulin, Beta) in samples from Serum, Plasma, Cell supernatant
Description: Recombinant NAP-2 is a disulfide-linked monomeric protein consisting of 71 amino acid residues and migrates as an approximately 8 kDa protein under non-reducing conditions and reducing conditions in SDS-PAGE. Optimized DNA sequence encoding Human NAP-2 (CXCL7) mature chain was expressed in E. coli.
Description: Recombinant NAP-2 is a disulfide-linked monomeric protein consisting of 71 amino acid residues and migrates as an approximately 8 kDa protein under non-reducing conditions and reducing conditions in SDS-PAGE. Optimized DNA sequence encoding Human NAP-2 (CXCL7) mature chain was expressed in E. coli.
