Human brain glial cells synthesize thrombospondin.

Asch, Adam S.; Leung, Lawrence L.K.; Shapiro, Joan Rankin; Nachman, Ralph L.

doi:10.1073/pnas.83.9.2904

Cited by 102 publications

(75 citation statements)

References 44 publications

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“…Thrombospondin expression is already pronounced during the proliferation and migration of the neuroepithelium, and continues to be prominent as neurons begin to differentiate and extend their processes. To what extent glial cells contribute to the diffuse staining of the neuropil is difficult to assess; however, Asch et al (1986) have reported that thrombospondin is synthesized by glial cells in vitro.…”

Section: Discussionmentioning

confidence: 99%

Colocalization of thrombospondin and syndecan during murine development

Corless

Mendoza

Collins

et al. 1992

Developmental Dynamics

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Thrombospondin is an adhesive glycoprotein that is thought to play a role in tissue genesis and repair. We have used a monoclonal anti-thrombospondin antibody, designated 5Gl1, to localize thrombospondin in paraformaldehyde fixed, paraffin-embedded sections of developing mouse embryos. Thrombospondin expression is observed in uterine smooth muscle, endometrial glands, the decidua, and trophoblastic giant cells during the initial phase of post-implantation development in the embryo. Cardiac myocytes and neuroepithelial cells show positive staining for thrombospondin at day 8.5 of gestation, and this expression continues throughout the development of the myocardium and central nervous system. Strong staining for thrombospondin is seen in developing bone and in the liver. Thrombospondin is also observed in developing smooth muscle and skeletal muscle, as well as in a variety of epithelia, including the epidermis, small intestinal epithelium, lens epithelium, renal tubular epithelium, and the epithelium of the developing tooth. Comparison of thrombospondin staining with that of two known cell surface receptors for thrombospondin, syndecan and the vitronectin receptor, reveals remarkable colocalization of thrombospondin and syndecan in all tissues, but almost no coexpression with the vitronectin receptor. Coexpression of thrombospondin and syndecan may play an important role in cell-cell or cell-matrix interactions during development. 0 1992 Wiley-Liss, Inc.

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Section: Discussionmentioning

confidence: 99%

Colocalization of thrombospondin and syndecan during murine development

Corless

Mendoza

Collins

et al. 1992

Developmental Dynamics

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“…Although TSP is a major platelet a-granule protein (3), is produced by a variety of cells in culture (5)(6)(7)(8), and is a component of the extracellular matrix (39), the biological role of this multifunctional glycoprotein is largely unknown. An adhesive function is suggested by its lectin activity (13) (it agglutinates fixed erythrocytes) and its demonstrated role in stabilizing platelet aggregation (4).…”

Section: Discussionmentioning

confidence: 99%

“…Although circulating plasma concentrations are low (2), it is a major a-granule protein of human platelets (3) and upon stimulation is expressed on the platelet surface where it stabilizes platelet aggregation (4). In addition, TSP is synthesized by fibroblasts, endothelial cells, aortic smooth muscle cells, and glial cells in culture and is incorporated into their extracellular matrices (5)(6)(7)(8). The biological role ofextra-platelet TSP is unknown, although it has been shown to interact specifically with several macromolecules including fibrinogen, fibronectin (FN), type V collagen, and heparin (9)(10)(11)(12) and to have lectin-like activity (13).…”

Section: Introductionmentioning

confidence: 99%

Thrombospondin binds to monocytes-macrophages and mediates platelet-monocyte adhesion.

Silverstein¹,

Nachman²

1987

J. Clin. Invest.

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129

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“…Oligodendrocytes isolated in bulk from adult normal rat or human brain can also be maintained in culture (Kim, McMorris & Sprinkle, 1984;Kim, 1985). Although glial fibrillary acidic protein (GFAP) antisera has been used to detect astrocytes in subcultures, little immunocytochemistry has been carried out on primary cultures from normal adult human brain (Rorke et al, 1975;Gilden et al, 1976;Barna et al, 1985;Asch et al, 1986;Cheng-Mayer et al, 1987).…”

Section: Introductionmentioning

confidence: 99%

Immunocytochemical Characterization of Primary Glial Cell Cultures From Normal Adult Human Brain

Newcombe¹,

Meeson

Cuzner

1988

Neuropathology Appl Neurobio

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Newcombe J., Meeson A. & Cuzner M. L. (1988) Neuropathology and Applied Neurobiology 14, 453–465 Immunocytochemical characterization of primary glial cell cultures from normal adult human brain Primary cultures were established from autopsy or biopsy samples of normal adult human brain and characterized by immunocytochemical techniques. Initially, macrophages were the predominant cell type adhering to the substratum, but as their number fell that of glial cells increased. Oligodendrocytes comprised 30% of the glial population in white matter cultures, and their perikarya and elongated processes were immunostained with antibodies directed against galactocerebroside and four myelin proteins. In white and grey matter cultures, process–bearing astrocytes and small numbers of polygonal astrocytes were stained with antibodies against glial fibrillary acidic protein and glutamine synthetase. Fibroblasts started to appear at 3 weeks and proliferated to form a monolayer beneath glial cells by 5 weeks. Glia began to die in the 6th week. These primary cell cultures of white or grey matter can be used to study the properties of glial cells from normal or pathological adult human brain.

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Human brain glial cells synthesize thrombospondin.

Cited by 102 publications

References 44 publications

Colocalization of thrombospondin and syndecan during murine development

Colocalization of thrombospondin and syndecan during murine development

Thrombospondin binds to monocytes-macrophages and mediates platelet-monocyte adhesion.

Immunocytochemical Characterization of Primary Glial Cell Cultures From Normal Adult Human Brain

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