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Tmem27: a cleaved and shed plasma membrane protein that stimulates pancreatic beta cell proliferation

Pinar Akpinar1, Satoru Kuwajima, Jan Krützfeldt

  • 1Laboratory of Metabolic Diseases, The Rockefeller University, 1230 York Avenue, New York, New York 10021, USA.

Cell Metabolism
|December 7, 2005
PubMed

Insights

Researchers identified transmembrane protein 27 (Tmem27) as a key regulator of pancreatic beta cell replication. Increased Tmem27 expression boosts beta cell growth, while its reduction impairs replication, offering insights into diabetes research.

Area of Science:

  • Endocrinology
  • Molecular Biology
  • Cell Biology

Background:

  • The regulation of terminally differentiated beta cell replication remains largely unknown.
  • Understanding these mechanisms is crucial for addressing beta cell dysfunction in diseases like diabetes.

Purpose of the Study:

  • To identify and characterize novel molecular regulators of pancreatic beta cell replication.
  • To investigate the role of transmembrane protein 27 (Tmem27) in beta cell growth.

Main Methods:

  • Utilized mouse models (Tcf1(-/-) and hypertrophy models) to study Tmem27 expression.
  • Employed RNA interference (RNAi) to silence Tmem27 and assessed thymidine incorporation.
  • Generated transgenic mice with altered Tmem27 expression in pancreatic beta cells.

Main Results:

  • Identified and characterized transmembrane protein 27 (Tmem27, also known as collectrin) in pancreatic beta cells.
  • Tmem27 expression is modulated in specific mouse models, correlating with endocrine pancreas hypertrophy.
  • Tmem27 undergoes beta cell-specific glycosylation, cleavage, and shedding.
  • Overexpression of full-length Tmem27 promotes beta cell replication (thymidine incorporation), while Tmem27 silencing reduces it.
  • Transgenic mice with elevated Tmem27 show increased beta cell mass.

Conclusions:

  • Transmembrane protein 27 (Tmem27) is a novel regulator of pancreatic beta cell replication and growth.
  • Tmem27's function in beta cell proliferation is linked to its full-length, membrane-bound form.
  • This discovery provides a new target for understanding and potentially treating conditions involving beta cell mass regulation.

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