Aortic Carboxypeptidase-Like Protein (ACLP): What is a Protein with a Name Like That Doing in Adipose Tissue?

Introduction

Aortic carboxypeptidase-like protein (ACLP) was originally cloned from aortic vascular smooth-muscle cells. It has been chosen as a subject for a hypothesis paper in this current issue of the journal due to its recent identification as a protein that is also expressed in adipose cells. Current data indicate its expression is downregulated during the early phase of the differentiation of fibroblast-like preadipose cells into mature adipose cells (adipogenesis). Remodeling the extracellular matrix (ECM) is a critical early event in adipogenesis, and ACLP may have the potential to interact with matrix components.

References

• 1 Layne M D, Endege W O, Jain M K, Yet S-F, Hsieh C-M, Chin M T. et al . Aortic carboxypeptidase-like protein, a novel protein with discoidin and carboxypeptidase-like domains, is up-regulated during vascular smooth muscle cell differentiation.  J Biol Chem. 1998;  273 15 654-15 660
• 2 Novikova E G, Reznik S E, Varlamov O, Fricker L D. Carboxypeptidase Z is present in the regulated secretory pathway and extracellular matrix in cultured cells and in human tissues.  J Biol Chem. 2000;  275 4865-4870
• 3 Layne M D, Yet S-F, Maemura K, Hsieh C-M, Bernfield M, Perrella M A. et al . Impaired abdominal wall development and deficient wound healing in mice lacking aortic carboxypeptidase-like protein.  Mol Cell Biol. 2001;  21 5256-5261
• 4 Vogel W, Gish G D, Alves F, Pawson T. The discoidin domain receptor tyrosine kinases are activated by collagen.  Mol Cell. 1997;  1 13-23
• 5 Shrivastava A, Radziejewski C, Campbell E, Kovac L, McGlynn M, Ryan T E. et al . An orphan receptor tyrosine kinase family whose members serve as nonintegrin collagen receptors.  Mol Cell. 1997;  1 25-34
• 6 He G-P, Muise A, Li A W, Ro H-S. A eukaryotic transcriptional repressor with carboxypeptidase activity.  Nature. 1995;  378 92-96
• 7 Song L, Fricker L D. Cloning and expression of human carboxypeptidase Z, a novel metallocarboxypeptidase.  J Biol Chem. 1997;  272 10 543-10 550
• 8 Ro H-S, Kim S-W, Wu D, Webber C, Nicholson T E. Gene structure and expression of the mouse adipocyte enhancer-binding protein.  Gene. 2001;  280 123-133
• 9 Rosen E D, Walkey C J, Puigserver P, Spiegelman B M. Transcriptional regulation of adipogenesis.  Genes Dev. 2000;  14 1293-1307
• 10 Soukas A, Socci N D, Saatkamp B D, Novelli S, Friedman J M. Distinct transcriptional profiles of adipogenesis in vivo and in vitro.  J Biol Chem. 2001;  276 34 167-34 174
• 11 Ross S E, Erickson R L, Gerin I, DeRose P M, Bajnok L, Longo K A. et al . Microarray analyses during adipogenesis: Understanding the effects of Wnt signaling on adipogenesis and the roles of liver X receptor a in adipocyte metabolism.  Mol Cell Biol. 2002;  22 5989-5999
• 12 Hauner H, Skurk T, Wabitsch M. Cultures of human adipose precursor cells.  Methods Mol Biol. 2001;  155 239-247
• 13 Gregoire F M, Smas C M, Sul H S. Understanding adipocyte differentiation.  Physiol Rev. 1998;  78 783-809
• 14 Lin F-T, Lane M D. CCAAT/enhancer binding protein a is sufficient to initiate the 3T3-L1 adipocyte differentiation program.  Proc Natl Acad Sci USA. 1994;  91 8757-8761
• 15 Shao D, Lazar M A. Peroxisome proliferator activated receptor g, CCAT/Enhancer-binding protein a, and cell cycle status regulate the commitment to adipocyte differentiation.  J Biol Chem. 1997;  272 21 473-21 478
• 16 El-Jack A K, Hamm J K, Pilch P F, Farmer S R. Reconstitution of insulin-sensitive glucose transport in fibroblasts requires expression of both PPARg and C/EBPa.  J Biol Chem. 1999;  274 7946-7951
• 17 Wu Z, Rosen E D, Brun R, Hauser S, Adelmant G, Troy A E. et al . Cross-regulation of C/EBPa and PPARg controls the transcriptional pathway of adipogenesis and insulin sensitivity.  Mol Cell. 1999;  3 151-158
• 18 Qiu Z, Wei Y, Chen N, Jiang M, Wu J, Liao K. DNA synthesis and mitotic clonal expansion is not a required step for 3T3-L1 preadipocyte differentiation into adipocytes.  J Biol Chem. 2001;  276 11 988-11 995
• 19 Hauner H. Complete adipose differentiation of 3T3-L1 cells in a chemically defined medium: comparison to serum-containing culture conditions.  Endocrinology. 1990;  127 865-872
• 20 Kuri-Harcuch W, Marsch-Moreno M. DNA synthesis and cell division related to adipose differentiation of 3T3 cells.  J Cell Physiol. 1983;  114 39-44
• 21 Yeh W-C, Bierer B E, McKnight S L. Rapamycin inhibits clonal expansion and adipogenic differentiation of 3T3-L1 cells.  Proc Natl Acad Sci USA. 1995;  92 11 086-11 090
• 22 Gagnon A, Abbaiian K J, Crapper T, Layne M D, Sorisky A. Down-regulation of aortic carboxypeptidase-like protein during the early phase of 3T3-L1 adipogenesis.  Endocrinology. 2002;  143 2478-2485
• 23 Richon V M, Lyle R E, McGehee R E. Regulation and expression of retinoblastoma proteins p107 and p130 during 3T3-L1 adipocyte differentiation.  J Biol Chem. 1997;  272 10 117-10 124
• 24 Springer W R, Cooper D N, Barondes S H. Discoidin I is implicated in cell-substratum attachment and ordered cell migration of Dictyostelium and resembles fibronectin.  Cell. 1984;  39 557-564
• 25 Spiegelman B M, Ginty C A. Fibronectin modulation of cell shape and lipogenic gene expression in 3T3-adipocytes.  Cell. 1983;  35 657-666
• 26 Ignotz R A, Massague J. Type b transforming growth factor controls the adipogenic differentiation of 3T3 fibroblasts.  Proc Natl Acad Sci USA. 1985;  82 8530-8534
• 27 Gagnon A M, Chabot J, Pardasani D, Sorisky A. Extracellular matrix induced by TGFb impairs insulin sugnal transduction in 3T3-L1 preadipose cells.  J Cell Physiol. 1998;  175 370-378
• 28 Saltiel A. You are what you secrete.  Nature Med. 2001;  7 887-888
• 29 Kratchmarova I, Kalume D E, Blagoev B, Scherer P E, Podtelejnikov A V, Molina H. et al . A proteomics approach for identification of secreted proteins during the differentiation of 3T3-L1 preadipocytes to adipocytes.  Mol Cell Proteomics. 2002;  1 213-222