High impact information on Crip2

• Co-transfection of CRP2 and cGKIbeta into COS cells confirmed the phosphorylation of CRP2 in vivo [1].
• The co-localization together with the specific phosphorylation of CRP2 by cGKI in vitro and in vivo suggests that CRP2 is a novel substrate of cGKI in neurons and smooth muscle of the small intestine [1].
• Cyclic GMP kinase I phosphorylated CRP2 at Ser-104, because the mutation to Ala completely prevented the in vivo phosphorylation [1].
• Immunohistochemical analysis using confocal laser scan microscopy showed a co-localization of CRP2 and cGKI in the inner part of the circular muscle layer, in the muscularis mucosae, and in specific neurons of the myenteric and submucosal plexus [1].
• No alternative splicing was observed for the CRP-2 mRNA [2].

Biological context of Crip2

• The ubiquitous tissue distribution and high level of expression of CRP2 mRNA suggest an important role for CRP2 in cell functions [3].
• It encodes a protein, denoted cysteine-rich protein 2 (CRP2), of 208 amino acid residues containing two tandem repeats of an unusual LIM/double zinc-finger-like motif [3].

Anatomical context of Crip2

• Cysteine-rich protein 2, a novel substrate for cGMP kinase I in enteric neurons and intestinal smooth muscle [1].

Analytical, diagnostic and therapeutic context of Crip2

• Among the changes observed following array analysis, increased nerve-growth-factor-induced B (NGFI-B), adenylyl cyclase type VIII (AC VIII), and reduced cysteine-rich protein 2 (CRP2) mRNA were confirmed by quantitative RT-PCR [4].

References