title: Comprehensive characterization of expression patterns of protein 4.1 family members in mouse adrenal gland: implications for functions.
abstract: The members of the protein 4.1 family, 4.1R, 4.1G, 4.1N, and 4.1B, are encoded by four genes, all of which undergo complex alternative splicing. It is well established that 4.1R, the prototypical member of the family, serves as an adapter that links the spectrin-actin based cytoskeleton to the plasma membrane in red cells. It is required for mechanical resilience of the membrane, and it ensures the cell surface accumulation of selected membrane proteins. However, the function of 4.1 proteins outside erythrocytes remains under-explored, especially in endocrine tissues. Transcripts of all 4.1 homologs have previously been documented to be abundantly expressed in adrenal gland. In order to begin to decipher the function of 4.1 proteins in adrenal gland, we performed a detailed characterization of the expression pattern of various 4.1 proteins and their cellular localization. We show that 4.1R (~80 and ~135 kDa) splice forms are expressed on the membrane of all cells, while a ~160 kDa 4.1G splice form is distributed in the cytoplasm and the membrane of zona glomerulosa and of medullary cells. Two 4.1N splice forms, ~135 and ~95 kDa, are present in the peri-nuclear region of both zona glomerulosa and medullary cells, while a single ~130 kDa 4.1B splice form, is detected in all layers of adrenal gland in both the cytoplasm and the membrane. The characterization of distinct splice forms of various 4.1 proteins with diverse cellular and sub-cellular localization indicates multiple functions for this family of proteins in endocrine functions of adrenal gland.
authors.affiliation: Red Cell Physiology Laboratory, New York Blood Center, 310 East 67th St, New York, NY 10065, USA.
authors.forename: Hua
authors.initials: H
authors.lastname: Wang
authors.forename: Congrong
authors.initials: C
authors.lastname: Liu
authors.forename: Gargi
authors.initials: G
authors.lastname: Debnath
authors.forename: Anthony J
authors.initials: AJ
authors.lastname: Baines
authors.forename: John G
authors.initials: JG
authors.lastname: Conboy
authors.forename: Narla
authors.initials: N
authors.lastname: Mohandas
authors.forename: Xiuli
authors.initials: X
authors.lastname: An
mesh_terms: D000199:Actins / Q000378:metabolism; D000311:Adrenal Glands / Q000378:metabolism*; D000818:Animals; D001798:Blood Proteins / Q000235:genetics / Q000378:metabolism*; D015153:Blotting, Western; D002448:Cell Adhesion; D002462:Cell Membrane / Q000235:genetics / Q000378:metabolism; D003598:Cytoskeletal Proteins / Q000235:genetics / Q000378:metabolism*; D004912:Erythrocytes; D015870:Gene Expression; D007150:Immunohistochemistry; D008565:Membrane Proteins / Q000235:genetics / Q000378:metabolism*; D051379:Mice; D008810:Mice, Inbred C57BL; D008840:Microfilament Proteins; D009479:Neuropeptides / Q000235:genetics / Q000378:metabolism*; D020133:Reverse Transcriptase Polymerase Chain Reaction; D013049:Spectrin / Q000378:metabolism
chemical_list: D000199:Actins; D001798:Blood Proteins; D003598:Cytoskeletal Proteins; C540651:Epb4.1l2 protein, mouse; C514956:Epb41 protein, mouse; C488402:Epb41l3 protein, mouse; D008565:Membrane Proteins; D008840:Microfilament Proteins; D009479:Neuropeptides; C120557:erythrocyte membrane protein band 4.1-like 1; D013049:Spectrin