The connexin43-interacting protein, CIP85, mediates the internalization of connexin43 from the plasma membrane.

CIP85 was previously identified as a connexin43 (Cx43)-interacting protein that is ubiquitously expressed in multiple mammalian tissues and cell types. The interaction between the SH3 domain of CIP85 and a proline-rich region of Cx43 has previously been associated with an increased rate of Cx43 turnover through lysosomal mechanisms. This report presents biochemical and immunofluorescence evidence that overexpression of CIP85 reduced the presence of Cx43 in gap junction plaques at the plasma membrane.

Degradation of connexins through the proteasomal, endolysosomal and phagolysosomal pathways.

Connexins comprise gap junction channels, which create a direct conduit between the cytoplasms of adjacent cells and provide for intercellular communication. Therefore, the level of total cellular connexin protein can have a direct influence on the level of intercellular communication. Control of connexin protein levels can occur through different mechanisms during the connexin life cycle, such as by regulation of connexin gene expression and turnover of existing protein.

Monoclonal antibodies against the connexin43-interacting protein CIP85.

The connexin43 (Cx43)-interacting protein of 85 kDa CIP85 has been identified as an interacting partner for the cytoplasmically located, carboxyl-terminal tail of Cx43. Further characterization has shown that the interaction between Cx43 and CIP85 is associated with increased turnover of Cx43 that may be lysosome-mediated. This suggests that CIP85 may regulate the endocytic trafficking of Cx43 from the plasma membrane and its degradation, and thus, indirectly influence gap junction function.

Compensatory paracrine mechanisms that define the urothelial response to injury in partial bladder outlet obstruction.

Diseases and conditions affecting the lower urinary tract are a leading cause of dysfunctional sexual health, incontinence, infection, and kidney failure. The growth, differentiation, and repair of the bladder's epithelial lining are regulated, in part, by fibroblast growth factor (FGF)-7 and -10 via a paracrine cascade originating in the mesenchyme (lamina propria) and targeting the receptor for FGF-7 and -10 within the transitional epithelium (urothelium). The FGF-7 gene is located at the 15q15-q21.

Induction of urothelial cell proliferation by fibroblast growth factor-7 in RAG1-deficient mice.

Fibroblast growth factor-7 (FGF-7, keratinocyte growth factor, KGF) is a 163 amino acid glycoprotein synthesized and secreted by mesenchymal cells (e.g. fibroblasts/fibrocytes) in epithelial organs, thereby functioning as a paracrine mediator of epithelial cell proliferation.