Bone and Mineral Metabolism: a brief note

Bone is a dynamic tissue that is remodeled constantly throughout life. The arrangement of compact and cancellous bone provides strength and density suitable for both mobility and protection. In addition, bone provides a reservoir for calcium, magnesium, phosphorus, sodium, and other ions necessary for homeostatic functions. Bone also hosts and regulates hematopoiesis by providing niches for hematopoietic cell proliferation and differentiation. The skeleton is highly vascular and receives about 10% of the cardiac output. Remodeling of bone is accomplished by two distinct cell types: osteoblasts produce bone matrix, and osteoclasts resorb the matrix.

The extracellular components of bone consist of a solid mineral phase in close association with an organic matrix, of which 90-95% is type I collagen. The noncollagenous portion of the organic matrix is heterogeneous and contains serum proteins such as albumin as well as many locally produced proteins, whose functions are incompletely understood. Those proteins include cell attachment/signaling proteins such as thrombospondin, osteopontin, and fibronectin; calcium-binding proteins such as matrix gla protein and osteocalcin; and proteoglycans such as biglycan and decorin. Some of the proteins organize collagen fibrils; others influence mineralization and binding of the mineral phase to the matrix.

The mineral phase is made up of calcium and phosphate and is best characterized as a poorly crystalline hydroxyapatite. The mineral phase of bone is deposited initially in intimate relation to the collagen fibrils and is found in specific locations in the “holes” between the collagen fibrils. This architectural arrangement of mineral and matrix results in a two-phase material well suited to withstand mechanical stresses. The organization of collagen influences the amount and type of mineral phase formed in bone. Although the primary structures of type I collagen in skin and bone tissues are similar, there are differences in posttranslational modifications and distribution of intermolecular cross-links. The holes in the packing structure of the collagen are larger in mineralized collagen of bone and dentin than in unmineralized collagens such as those in tendon. Single amino acid substitutions in the helical portion of either the α1 (COL1A1) or α2 (COL1A2) chains of type I collagen disrupt the organization of bone in osteogenesis imperfecta. The severe skeletal fragility associated with this group of disorders highlights the importance of the fibrillar matrix in the structure of bone.

Endocrinology and Metabolism: Open Access is a peer reviewed journal which focuses on the publication of current research and developments on the endocrine glands and its secretions with their coordination with metabolism and reproduction.

Endocrinology and Metabolism: Open Access Journal is using Editorial Tracking System to maintain quality and transparency to the author in the peer-review process. Review processing will be performed by the editorial board members of the Journal Endocrinology and Metabolism: Open Access or by Reviewers (outside experts in the field). Two independent reviewer’s approval (Minimum reviewer’s approval) followed by editor approval is obligatory for acceptance of any manuscript excluding an editorial.

Journal is now accepting manuscripts for volume 5 for year 2021. We publish minimum of 5 and maximum of 20 articles per issue every month. Submissions to our journal are given high priority during the process.

Submit your manuscript at:

https://www.imedpub.com/submissions/endocrinology-metabolism-open-access.html 

You may also send the manuscript as an attachment to mail endometabol@emedscholar.com

Media Contact
Eliza Grace
Associate Managing Editor
Endocrinology and Metabolism: Open Access
E-Mail: endometabol@emedscholar.com