GJA8

(redirected from cell surface glycoprotein)

GJA8

A gene on chromosome 1q21.1 that encodes a calcium and pH-dependent transmembrane connexin protein required for lens growth and maturation of lens-fibre cells. 

Molecular pathology
GJA8 mutations have been linked to zonular pulverulent cataracts, nuclear progressive cataracts, and cataract-microcornea syndrome.
Mentioned in ?
References in periodicals archive ?
The ubiquitous cell surface glycoprotein CD47 (integrin-associated protein) is an important regulator of integrin function, but it also interacts with other proteins, such as thrombospondins (TSP) and signal regulatory proteins (SIRP).
Mesothelin is a 40 kDa cell surface glycoprotein. The mesothelin gene is located on chromosome 16p13.3 and encodes at least four protein products, including megakaryocyte potentiating factor (MPF) [13, 14] and three isoforms of mesothelin, which are variant 1 (mesothelin) [14], the currently uncharacterized variant 2 [15, 16], and variant 3 (soluble-mesothelin-related protein (SMRP)) [17].
Katz, "Pemphigus antibodies identify a cell surface glycoprotein synthesized by human and mouse keratinocytes," Journal of Clinical Investigation, vol.
The MIC2 gene product is a cell surface glycoprotein found on ES cells and is very useful in the differential diagnosis.
The immunoreactivity of the tumor cells for vimentin and O13 antibody (also known as the Ewing/ PNET antigen) offers additional support for a diagnosis of EES and PNET O13 is a monoclonal antibody to a cell surface glycoprotein (p30/[32.sup.MIC2]) encoded by the pseudoautosomal MIC2 gene on the X and Y chromosomes.
Cell-cell binding is mediated by a cell surface glycoprotein. Binding between these molecules (gp80) on adjacent cells is associated with an interdigitation of filopodia unlike any cell junctions in animals (Siu et al., 1988; Gerisch, 1986).
(2) The immunohistochemical profile of ES includes strong reactivity to the cell surface glycoprotein CD99 antigen, encoded by the pseudoautosomal MIC-2 gene.
The presence of the bisecting GlcNAc on the cell surface glycoproteins affects their interaction with galectins and siglecs, probably altering N-glycan conformation (92).
(3) These observations sparked extensive investigations of glycoconjugates of malignant cells, and soon many investigators demonstrated that both quantitative and qualitative changes take place in cell surface glycoproteins and glycosphingolipids (GSLs) upon malignant transformation of cells.