title: Transient expression of cellular retinol-binding protein-1 during cardiac repair after myocardial infarction.
abstract: Retinoic acid (RA) is a vitamin A derivative that exerts pleiotropic biological effects. Intracellular transport and metabolism of RA are regulated by cellular retinol-binding proteins (CRBP). CRBP-1 is transiently expressed in granulation tissue fibroblasts during wound healing; however, its role in cardiac remodeling remains unknown. A rat myocardial infarction (MI) model was established by ligation of the left coronary artery, and hearts were obtained at 3, 6, 15, 30 and 45 days after operation. Heart sections were examined immunohistochemically using anti-vimentin, anti-α-smooth muscle actin (α-SMA), anti-matrix metalloproteinase (MMP)-2, anti-MMP-9 and anti-CRBP-1 antibodies. Infarction involved 48.8 ± 3.6% of the left ventricle and was followed by an important cardiac remodeling. Vimentin-positive fibroblastic cells including α-SMA-positive myofibroblasts expressed CRBP-1 at 3-, 6-, and 15-days after MI. Expression of CRBP-1 reached a maximum at 6-days after infarction. Thereafter, CRBP-1 expression was dramatically decreased, showing a similar tendency to MMP expression. Human heart specimens of individuals with a recent myocardial infarction demonstrated presence of CRBP-1-positive fibroblasts by immunohistochemistry. We have demonstrated that CRBP-1 is transiently expressed by fibroblasts during cardiac remodeling. Our results suggest that CRBP-1 plays a role in ventricular remodeling after MI allegedly through its RA binding activity.
authors.affiliation: Department of Pathology, National Cerebral and Cardiovascular Center, Osaka, Japan.
authors.forename: Mengyue
authors.initials: M
authors.lastname: Yu
authors.forename: Hatsue
authors.initials: H
authors.lastname: Ishibashi-Ueda
authors.forename: Keiko
authors.initials: K
authors.lastname: Ohta-Ogo
authors.forename: Giulio
authors.initials: G
authors.lastname: Gabbiani
authors.forename: Masakazu
authors.initials: M
authors.lastname: Yamagishi
authors.forename: Kenshi
authors.initials: K
authors.lastname: Hayashi
authors.forename: Seiichi
authors.initials: S
authors.lastname: Hirota
authors.forename: Marie-Luce
authors.initials: ML
authors.lastname: Bochaton-Piallat
authors.forename: Hiroyuki
authors.initials: H
authors.lastname: Hao
mesh_terms: D000199:Actins / Q000378:metabolism; D000368:Aged; D000818:Animals; D015415:Biomarkers / Q000378:metabolism; D004195:Disease Models, Animal; D005347:Fibroblasts / Q000378:metabolism / Q000473:pathology; D006352:Heart Ventricles / Q000378:metabolism; D006801:Humans; D008297:Male; D020778:Matrix Metalloproteinase 2 / Q000378:metabolism; D020780:Matrix Metalloproteinase 9 / Q000378:metabolism; D009203:Myocardial Infarction / Q000378:metabolism* / Q000473:pathology; D009206:Myocardium / Q000378:metabolism* / Q000473:pathology; D032383:Myocytes, Cardiac / Q000378:metabolism / Q000473:pathology; D051381:Rats; D017208:Rats, Wistar; D054840:Retinol-Binding Proteins, Cellular / Q000378:metabolism*; D020257:Ventricular Remodeling / Q000502:physiology*; D014746:Vimentin / Q000378:metabolism
chemical_list: C541116:ACTA2 protein, human; D000199:Actins; D015415:Biomarkers; D054840:Retinol-Binding Proteins, Cellular; D014746:Vimentin; D020778:Matrix Metalloproteinase 2; D020780:Matrix Metalloproteinase 9