Matrix metalloproteinases and bone.
Matrix metalloproteinases (MMPs) are members of a family of zinc-dependent proteolytic enzymes. Several of the MMPs are expressed at high levels in bone and cartilage in mammals including humans and mice and are capable of cleaving native, undenatured collagens with long uninterrupted triple helices; these MMPs therefore potentially function as collagenases in vivo. Several MMPs expressed in the skeleton appear to function in endochondral ossification during embryonic development and in modeling and remodeling of bone postnatally and later in life. Different functions of MMPs have been elucidated through observations of spontaneous mutations in MMP genes in humans and of targeted mutations in Mmp genes and collagen (substrate) genes in mice. Potential mechanisms to account for effects of these mutations are considered in this review.
Krane
Stephen M
SM
Department of Medicine, Harvard Medical School and the Massachusetts General Hospital, Center for Immunology and Inflammatory Diseases, Building 149 13th Street, Room 8301, Boston. MA 02129, USA. Electronic address: krane.stephen@mgh.harvard.edu.
Inada
Masaki
M
Department of Medicine, Harvard Medical School and the Massachusetts General Hospital, Center for Immunology and Inflammatory Diseases, Building 149 13th Street, Room 8301, Boston. MA 02129, USA.
D000595:Amino Acid Sequence; D000818:Animals; D001842:Bone and Bones / Q000201:enzymology*; D003094:Collagen / Q000235:genetics; D006801:Humans; D020782:Matrix Metalloproteinases / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D008969:Molecular Sequence Data; D009154:Mutation
D003094:Collagen; D020782:Matrix Metalloproteinases