Immunolocalization of matrix metalloproteinase-13 on bone surface under osteoclasts in rat tibia

Hiroaki Nakamura, Ginga Sato, Azumi Hirata, Toshio Yamamoto

Research output: Contribution to journalArticle

52 Citations (Scopus)

Abstract

Matrix metalloproteinase (MMP)-13 (an interstitial collagenase also called collagenase 3) is involved in degradation of extracellular matrix in various tissues. Using immunohistochemistry and Western blotting, we investigated localization of MMP-13 in rat tibia, to clarify the role of MMP-13 in bone resorption. MMP-13 reactivity was mainly seen on bone surfaces under osteoclasts, and in some osteocytes and their lacunae near osteoclasts. However, immunoreactivity was not seen in chondrocytes or osteoclasts. MMP-13 was also localized on cement lines in the epiphysis. In the growth plate erosion zone, perivascular cells showed MMP-13 reactivity. Immunoelectron microscopy revealed that MMP-13 was localized on the bone surfaces, under the ruffled borders and some clear zones of osteoclasts. Gold-labeled MMP-13 was closely associated with collagen fibrils. Gold labeling was also detected in Golgi apparatus of osteocytes adjacent to osteoclasts and bone lining cells. Western blotting showed that MMP-13 was mainly associated with mineralized bone matrix. These findings suggest that MMP-13 synthesized and secreted by osteoblast-lineage cells is localized under the ruffled borders of osteoclasts. MMP-13 may play an important role in degradation of type I collagen in bone matrix, acting in concert with cathepsin K and MMP-9 produced by osteoclasts. MMP-13 in perivascular cells may be involved in removal of cartilage matrix proteins such as type II collagen and aggrecan.

Original languageEnglish
Pages (from-to)48-56
Number of pages9
JournalBone
Volume34
Issue number1
DOIs
Publication statusPublished - Jan 2004

Fingerprint

Matrix Metalloproteinase 13
Osteoclasts
Tibia
Bone and Bones
Osteocytes
Bone Matrix
Gold
Fibril-Associated Collagens
Matrilin Proteins
Western Blotting
Cathepsin K
Aggrecans
Matrix Metalloproteinase 1
Epiphyses
Growth Plate
Collagen Type II
Immunoelectron Microscopy
Matrix Metalloproteinase 9
Golgi Apparatus
Bone Resorption

Keywords

  • Cartilage matrix proteins
  • Matrix metalloproteinase
  • Rat tibia

ASJC Scopus subject areas

  • Physiology
  • Hematology

Cite this

Immunolocalization of matrix metalloproteinase-13 on bone surface under osteoclasts in rat tibia. / Nakamura, Hiroaki; Sato, Ginga; Hirata, Azumi; Yamamoto, Toshio.

In: Bone, Vol. 34, No. 1, 01.2004, p. 48-56.

Research output: Contribution to journalArticle

Nakamura, Hiroaki ; Sato, Ginga ; Hirata, Azumi ; Yamamoto, Toshio. / Immunolocalization of matrix metalloproteinase-13 on bone surface under osteoclasts in rat tibia. In: Bone. 2004 ; Vol. 34, No. 1. pp. 48-56.
@article{f18837c2b86e45d583fdb340bd0c4371,
title = "Immunolocalization of matrix metalloproteinase-13 on bone surface under osteoclasts in rat tibia",
abstract = "Matrix metalloproteinase (MMP)-13 (an interstitial collagenase also called collagenase 3) is involved in degradation of extracellular matrix in various tissues. Using immunohistochemistry and Western blotting, we investigated localization of MMP-13 in rat tibia, to clarify the role of MMP-13 in bone resorption. MMP-13 reactivity was mainly seen on bone surfaces under osteoclasts, and in some osteocytes and their lacunae near osteoclasts. However, immunoreactivity was not seen in chondrocytes or osteoclasts. MMP-13 was also localized on cement lines in the epiphysis. In the growth plate erosion zone, perivascular cells showed MMP-13 reactivity. Immunoelectron microscopy revealed that MMP-13 was localized on the bone surfaces, under the ruffled borders and some clear zones of osteoclasts. Gold-labeled MMP-13 was closely associated with collagen fibrils. Gold labeling was also detected in Golgi apparatus of osteocytes adjacent to osteoclasts and bone lining cells. Western blotting showed that MMP-13 was mainly associated with mineralized bone matrix. These findings suggest that MMP-13 synthesized and secreted by osteoblast-lineage cells is localized under the ruffled borders of osteoclasts. MMP-13 may play an important role in degradation of type I collagen in bone matrix, acting in concert with cathepsin K and MMP-9 produced by osteoclasts. MMP-13 in perivascular cells may be involved in removal of cartilage matrix proteins such as type II collagen and aggrecan.",
keywords = "Cartilage matrix proteins, Matrix metalloproteinase, Rat tibia",
author = "Hiroaki Nakamura and Ginga Sato and Azumi Hirata and Toshio Yamamoto",
year = "2004",
month = "1",
doi = "10.1016/j.bone.2003.09.001",
language = "English",
volume = "34",
pages = "48--56",
journal = "Bone",
issn = "8756-3282",
publisher = "Elsevier Inc.",
number = "1",

}

TY - JOUR

T1 - Immunolocalization of matrix metalloproteinase-13 on bone surface under osteoclasts in rat tibia

AU - Nakamura, Hiroaki

AU - Sato, Ginga

AU - Hirata, Azumi

AU - Yamamoto, Toshio

PY - 2004/1

Y1 - 2004/1

N2 - Matrix metalloproteinase (MMP)-13 (an interstitial collagenase also called collagenase 3) is involved in degradation of extracellular matrix in various tissues. Using immunohistochemistry and Western blotting, we investigated localization of MMP-13 in rat tibia, to clarify the role of MMP-13 in bone resorption. MMP-13 reactivity was mainly seen on bone surfaces under osteoclasts, and in some osteocytes and their lacunae near osteoclasts. However, immunoreactivity was not seen in chondrocytes or osteoclasts. MMP-13 was also localized on cement lines in the epiphysis. In the growth plate erosion zone, perivascular cells showed MMP-13 reactivity. Immunoelectron microscopy revealed that MMP-13 was localized on the bone surfaces, under the ruffled borders and some clear zones of osteoclasts. Gold-labeled MMP-13 was closely associated with collagen fibrils. Gold labeling was also detected in Golgi apparatus of osteocytes adjacent to osteoclasts and bone lining cells. Western blotting showed that MMP-13 was mainly associated with mineralized bone matrix. These findings suggest that MMP-13 synthesized and secreted by osteoblast-lineage cells is localized under the ruffled borders of osteoclasts. MMP-13 may play an important role in degradation of type I collagen in bone matrix, acting in concert with cathepsin K and MMP-9 produced by osteoclasts. MMP-13 in perivascular cells may be involved in removal of cartilage matrix proteins such as type II collagen and aggrecan.

AB - Matrix metalloproteinase (MMP)-13 (an interstitial collagenase also called collagenase 3) is involved in degradation of extracellular matrix in various tissues. Using immunohistochemistry and Western blotting, we investigated localization of MMP-13 in rat tibia, to clarify the role of MMP-13 in bone resorption. MMP-13 reactivity was mainly seen on bone surfaces under osteoclasts, and in some osteocytes and their lacunae near osteoclasts. However, immunoreactivity was not seen in chondrocytes or osteoclasts. MMP-13 was also localized on cement lines in the epiphysis. In the growth plate erosion zone, perivascular cells showed MMP-13 reactivity. Immunoelectron microscopy revealed that MMP-13 was localized on the bone surfaces, under the ruffled borders and some clear zones of osteoclasts. Gold-labeled MMP-13 was closely associated with collagen fibrils. Gold labeling was also detected in Golgi apparatus of osteocytes adjacent to osteoclasts and bone lining cells. Western blotting showed that MMP-13 was mainly associated with mineralized bone matrix. These findings suggest that MMP-13 synthesized and secreted by osteoblast-lineage cells is localized under the ruffled borders of osteoclasts. MMP-13 may play an important role in degradation of type I collagen in bone matrix, acting in concert with cathepsin K and MMP-9 produced by osteoclasts. MMP-13 in perivascular cells may be involved in removal of cartilage matrix proteins such as type II collagen and aggrecan.

KW - Cartilage matrix proteins

KW - Matrix metalloproteinase

KW - Rat tibia

UR - http://www.scopus.com/inward/record.url?scp=0942278947&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0942278947&partnerID=8YFLogxK

U2 - 10.1016/j.bone.2003.09.001

DO - 10.1016/j.bone.2003.09.001

M3 - Article

C2 - 14751562

AN - SCOPUS:0942278947

VL - 34

SP - 48

EP - 56

JO - Bone

JF - Bone

SN - 8756-3282

IS - 1

ER -