molecular/cellular biology and pathologies associated with collagen
The goal of my research is to understand the regulation and function of
collagen. Collagen is a most abundant protein and it accounts for approximately 30% of the protein in the body. Forty five genes have so far been identified, which code α chains and generate 28 molecules. The collagen molecules have common structures. The α
chains are composed of s series of G-X-Y triplets (G: glycine, X and Y are any amino acid residue) and form a triple helix to further organize various fibrils together with other extracellular molecules. My career as a researcher started with the generation of an antibody against type VI collagen and an immunohistochemical examination of its distribution in tissues. I learned molecular biology, and cloned the genes coding for type XI and XIX collagen when was a postdoctoral fellow in the United States. I have continued to work on the expression, regulation, and signal transduction of collagen genes as well as on the function of the protein using a null mouse model. I am also investigating the mechanism of fibrosis and its application for therapy using an animal model.
Yano H, Hamanaka R, Nakamura-Ota M, Adachi S, Zhang JJ, Matsuo N, Yoshioka H: Sp7/Osterix induces the mouse pro-a2(I) collagen gene (Col1a2) expression via the proximal promoter in osteoblastic cells. BBRC 452, 531-536, 2014.
2)
Hida M, Hamanaka R, Okamoto O, Yamashita K, Sasaki T, Yoshioka H, Matsuo N: Nuclear factor Y (NF-Y) regulates the proximal promoter activity of the mouse collagen α1(XI) gene. In Vitro Cell Dev Biol – Animal 50, 358-366, 2014.
3)
Nakamura-Ota M, Hamanaka R, Yano H, Adachi S, Sumiyoshi H, Matsuo N, and Yoshioka H. A new murine osteoblastic cell line immortalized with the SV40 large T antigen. Cell Tissue Bank 15:373-380, 2014
4)
Yano
H, Hamanaka R, Nakamura N, Sumiyoshi H, Matsuo N, Yoshioka H: Smad, but
not MAPK, pathway mediates the expression of type I collagen in
radiation induced fibrosis. BBRC 418, 457-463, 2012.
5)
Wu
Y-F, Matsuo N, Sumiyoshi H, Yoshioka H: Sp7/Osterix is involved in the
up-regulation of the mouse pro-α1(V) collagen gene (Col5a1) in
osteoblastic cells. Matrix Biol. 29, 701-706, 2010.
6)
Wu,
Y.F., Matsuo, N., Sumiyoshi, H., Yoshioka, H .: Sp7/Osterix
up-regulates the mouse pro-a3(V) collagen gene
(Col5a3) during the osteoblast differentiation. BBRC 394,
503-508, 2010
7)
Hamada
Y, Sumiyoshi H, Matsuo N, Yun-Feng W, Nakashima M, Yanagisawa S,
Yoshioka H: The pro-a2(XI) collagen gene is expressed in odontoblasts.
BBRC 392, 166-170, 2010.
8)
Matsuo,
N., Tanaka, S, Yoshioka, H, Gordon, M.K., Ramirez, F.: Collagen XXIV
(Col24a1) gene expression is a specific marker of osteoblast
differentiation and bone formation. Connect. Tissue Res. 49: 68-75, 2008
9)
Matsuo,
N, Tanaka, S, Gordon, M.K., Koch, M., Yoshioka, H., Ramirez, F.:
CREB-AP1 protein complexes regulate transcription of the collagen XXIV
gene (Col24a1) in osteoblast. J. Biol. Chem. 281: 5445-5452, 2006
10)
Yamaguchi,
K., Matsuo, N., Sumiyoshi, H., Fujimoto, N., Iyama, K.-I., Yanagisawa,
S., Yoshioka, H.: The pro-α3(V) collagen chain is expressed in bone and
its N-terminal basic peptide is adhesive to osteosarcoma cells. Matrix
Biol: 24, 283-294, 2005
11)
Sumiyoshi,
H., Mor, N., Lee, S.Y., Doty, S., Henderson, S., Tanaka, S., Yoshioka,
H., Rattan, S., Ramirez, F.: Esophageal muscle physiology and
morphogenesis require assembly of a collagen XIX-rich basement membrane
zone. J. Cell Biol. 166: 591-600, 2004
12)
Nagato,
H., Matsuo, N., Sumiyoshi, H., Sakata-Takatani, K., Nasu, M., Yoshioka,
H.: The Transcription factor CCAAT-binding factor CBF/NF-Y and two
repressors regulate the core promoter of the human pro-α3(V)
collagen gene (COL5A3). J. Biol. Chem. 279: 46373-46383, 2004
13)
Sakata-Takatani,
K., Matsuo, N., Sumiyoshi, H., Tsuda, T., Yoshioka, H.: Identification
of a functional CCAAT-like motif in the core promoter of the mouse pro-α1(V)
collagen gene (Col5a1). Matrix Biol. 23: 87-99, 2004
14)
Matsuo,
N., Wang, Y.-H., Sumiyoshi, H., Sakata-Takatani, K., Nagato, H., Sakai,
K., Sakurai, M., Yoshioka, H.: The transcription factor CCAAT-binding
factor CBF/NF-Y regulates the proximal promoter activity in the
human α1(XI) collagen gene (COL11A1). J. Biol. Chem. 278:
32763-32770, 2003
15)
Iyama, K., Sumiyoshi, H., Khaleduzzaman, M.,
Matsuo, N., Yoshioka, H.: Differential expression of two exons of
the α1(XI) collagen gene (Col11a1) in the mouse embryo.
Matrix Biol. 20: 53-61, 2001
16)
Sumiyoshi,
H, Laub, F., Yoshioka, H., Ramirez, F.: Embryonic expression of type
XIX collagen is transient and confined to muscle cells. Dev. Dyn. 220:
155-162, 2001
17)
Kinoshita,
A., Greenwel, P., Tanaka, S., Di Liberto, M., Yoshioka, H., Ramirez,
F.: A transcription activator with restricted tissue distribution
regulates cell-specific expression of α1(XI)
collagen. J. Biol. Chem. 272: 31777-31784, 1997
18)
Khaleduzzaman,
M., Sumiyoshi, H., Ueki, Y., Inoguchi, K., Ninomiya, Y., Yoshioka, H.:
Structure of the human type XIX collagen (COL19A1) gene, which suggests
it has arisen from an ancestor gene of the FACIT family. Genomics 45:
304-312, 1997
19)
Sumiyoshi, H., Inoguchi, K., Khaleduzzaman, M.,
Ninomiya, Y. Yoshioka, H.: Ubiquitous expression of the α1(XIX)
collagen gene (Col19a1) during mouse embryogenesis becomes restricted
to a few tissues in the adult organism. J. Biol. Chem. 272:
17104-17111, 1997
20)
Inoguchi, K., Yoshioka, H., Khaleduzzaman, M.,
Ninomiya, Y.: The mRNA for α1(XIX)
collagen chain, a new member of FACITs, contains a long unusual 3'
untranslated region and displays many unique splicing variants. J.
Biochem. 117: 137-146, 1995
21)
Yoshioka,
H., Greenwel, P., Inoguchi, K., Truter, S., Inagaki, Y., Ninomiya, Y.,
Ramirez, F.: Structural and fanctional analysis of the promoter of the
human α1(XI) collagen gene. J. Biol. Chem. 270: 418-424,
1995
Yoshioka,
H., Iyama , K., Inoguchi, K., Khaleduzzaman, M., Ninomiya Y., Ramirez
F.: Developmental pattern of expression of the mouse α1(XI)
collagen gene (Col11a1). Dev. Dyn. 204: 41-47, 1995
24)
Yoshioka,
H., Zhang, H., Ramirez, F, Mattei, M.-G., Moradi-Ameli, M., van der
Rest M., Gordon, M.K.: Synteny between the loci for a novel FACIT-like
collagen locus (D6S228E) and α1(IX) collagen (COL9A1) on 6q12-q14 humans.
Genomics 13: 884-886, 1992
25)
Yoshioka, H., Ramirez, R.: Pro-α1(XI)
collagen : Structure of the amino-terminal propeptide and expression of
the gene in tumor cell lines. J. Biol. Chem. 265: 6423-6426, 1990
26)
Ramirez
F, Boast S, D'Alessio M, Lee B, Prince J, Su MW, Vissing H, Yoshioka H:
Fibrillar collagen genes. Structure and expression in normal and
diseased states. Ann N Y Acad Sci. 580, 74-80, 1990.
27)
Bernard,
M., Yoshioka, H., Rodriguez, E., van der Rest, M., Kimura, T.,
Ninomiya, Y., Olsen, B.R., Ramirez, F.: Cloning and sequencing of pro-α1(XI)
collagen cDNA demonstrates that type XI belongs to the fibrillar class
of collagens and reveals that the expression of the gene is not
restricted to cartilagenous tissue. J. Biol. Chem. 263: 17159-17166,
1988
28)
Oyamada
I, Kitaoka M, Araki C, Yoshioka H, Usuku G: Collagenase from the
culture medium of rabbit colon wall with special reference to the
latent type and substrate specificity. Gastroenterology 85, 376-384,
1983.
