In:
Biochemical Journal, Portland Press Ltd., Vol. 330, No. 3 ( 1998-03-15), p. 1255-1263
Abstract:
A new splice variant of the human integrin subunit β1 has been identified and designated β1C-2. It differs from the previously reported β1C (in this report designated β1C-1) by 18 nucleotides, and is generated by splicing from exon 6 to an alternative splice acceptor site within exon C, causing an in-frame deletion of six amino acids of the cytoplasmic region of β1C-1. The β1C-2 mRNA is present in several human cell lines and tissues at low levels, similarly to β1C-1. In peripheral T-lymphocytes, β1C-2 is the selectively expressed isoform. Neither β1C-1 nor β1C-2 mRNA could be detected in mouse tissues, and Southern hybridization of a mouse genomic β1 clone with a human exon-C-specific probe failed to identify a corresponding mouse exon. The antisense orientation of exon C is highly homologous to an Alu element. Since Alu elements are restricted to primates, the β1C-1 and β1C-2 variants of the integrin subunit β1 are specific for these species. The protein coded for by the β1C-2 cDNA can be expressed and localized to the surface of β1 deficient mouse cells. However, while stable transformed clones expressing high levels of the β1A were commonly found, the β1C-1 and β1C-2 expressing clones expressed barely detectable amounts of the β1 protein. Hence, high levels of β1C-2 may be incompatible with cell proliferation, as previously suggested for β1C-1.
Type of Medium:
Online Resource
ISSN:
0264-6021
,
1470-8728
Language:
English
Publisher:
Portland Press Ltd.
Publication Date:
1998
detail.hit.zdb_id:
1473095-9
SSG:
12
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