Immunohistochemical localization of S100 beta in human nervous system tumors by using monoclonal antibodies with specificity for the S100 beta polypeptide.

The immunohistochemical localization of the calcium-binding protein, S100 beta, in human nervous system tumors has been examined by using a monoclonal antibody with specificity for the S100 beta polypeptide. S100 beta-specific immunoreactivity is detected in astrocytoma, glioblastoma, Schwannoma, ependymoma, and craniopharyngioma, whereas no reactivity is seen in oligodendroglioma, meningioma, neuroblastoma, or medulloblastoma. These data suggest that analysis of S100 beta localization with these monoclonal antibodies may be useful for research or diagnostic purposes.

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Secreted modular calcium-binding protein 1 binds and activates thrombin to account for platelet hyperreactivity in diabetes

Blood ◽

10.1182/blood.2020009405 ◽

2021 ◽

Vol 137 (12) ◽

pp. 1641-1651

Author(s):

Fredy Delgado Lagos ◽

Amro Elgheznawy ◽

Anastasia Kyselova ◽

Dagmar Meyer zu Heringdorf ◽

Corina Ratiu ◽

...

Keyword(s):

Type 2 Diabetes ◽

Monoclonal Antibodies ◽

Platelet Function ◽

Calcium Binding ◽

Transforming Growth Factor ◽

Binding Protein ◽

Calcium Binding Protein ◽

Matricellular Protein

Abstract Secreted modular calcium-binding protein 1 (SMOC1) is an osteonectin/SPARC-related matricellular protein, whose expression is regulated by microRNA-223 (miR-223). Given that platelets are rich in miR-223, this study investigated the expression of SMOC1 and its contribution to platelet function. Human and murine platelets expressed SMOC1, whereas platelets from SMOC1+/− mice did not present detectable mature SMOC1 protein. Platelets from SMOC1+/− mice demonstrated attenuated responsiveness to thrombin (platelet neutrophil aggregate formation, aggregation, clot formation, Ca2+ increase, and β3 integrin phosphorylation), whereas responses to other platelet agonists were unaffected. SMOC1 has been implicated in transforming growth factor-β signaling, but no link to this pathway was detected in platelets. Rather, the SMOC1 Kazal domain directly bound thrombin to potentiate its activity in vitro, as well as its actions on isolated platelets. The latter effects were prevented by monoclonal antibodies against SMOC1. Platelets from miR-223–deficient mice expressed high levels of SMOC1 and exhibited hyperreactivity to thrombin that was also reversed by preincubation with monoclonal antibodies against SMOC1. Similarly, SMOC1 levels were markedly upregulated in platelets from individuals with type 2 diabetes, and the SMOC1 antibody abrogated platelet hyperresponsiveness to thrombin. Taken together, we have identified SMOC1 as a novel thrombin-activating protein that makes a significant contribution to the pathophysiological changes in platelet function associated with type 2 diabetes. Thus, strategies that target SMOC1 or its interaction with thrombin may be attractive therapeutic approaches to normalize platelet function in diabetes.

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Calcium-Binding Protein in the Central Nervous System and Other Tissues

Calcium in Biological Systems ◽

10.1007/978-1-4613-2377-8_55 ◽

1985 ◽

pp. 519-524

Author(s):

C. Owen Parkes

Keyword(s):

Central Nervous System ◽

Nervous System ◽

Calcium Binding ◽

Binding Protein ◽

Calcium Binding Protein ◽

The Central Nervous System

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Distribution of a specific calcium-binding protein of the S100 protein family, S100A6 (calcyclin), in subpopulations of neurons and glial cells of the adult rat nervous system

The Journal of Comparative Neurology ◽

10.1002/(sici)1096-9861(19990208)404:2<235::aid-cne8>3.0.co;2-7 ◽

1999 ◽

Vol 404 (2) ◽

pp. 235-257 ◽

Cited By ~ 36

Author(s):

Norifumi Yamashita ◽

Evelyn C. Ilg ◽

Beat W. Sch�fer ◽

Claus W. Heizmann ◽

Toshio Kosaka

Keyword(s):

Nervous System ◽

Glial Cells ◽

Calcium Binding ◽

Binding Protein ◽

S100 Protein ◽

Calcium Binding Protein ◽

Protein Family ◽

Adult Rat

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Calcium-binding protein of the chick chorioallantoic membrane. I. Immunohistochemical localization

The Journal of Cell Biology ◽

10.1083/jcb.77.3.743 ◽

1978 ◽

Vol 77 (3) ◽

pp. 743-751 ◽

Cited By ~ 23

Author(s):

RS Tuan ◽

WA Scott ◽

ZA Cohn

Keyword(s):

Calcium Binding ◽

Calcium Transport ◽

External Surface ◽

Binding Protein ◽

Chorioallantoic Membrane ◽

Immunohistochemical Localization ◽

Calcium Binding Protein ◽

Transport Function ◽

Chick Chorioallantoic Membrane

The preparation of a specific antiserum (anti-CaBP) against the calcium-binding protein (CaBP) of the chorioallantoic membrane (CAM) is described. The anti-CaBP appeared to be specific for the CaBP by immunodiffusion and immunoelectrophoresis. Application of the anti-CaBP in immunofluorescence histochemistry revealed that the CaBP is present in the CAM only at developmental ages corresponding with the expression of the calcium transport function of the membrane. Furthermore, the CaBP is localized to the ectoderm of the CAM, appears to be exposed to the entire external surface of the ectoderm, and can be shown to be associated with cells enzymatically dissociated from the CAM. These results are consistent with a functional role of the CaBP in the CAM calcium transport process.

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