Localization of PGI (biglycan, BGN) and PGII (decorin, DCN, PG-40) genes on human chromosomes Xq13-qter and 12q, respectively

doi:10.1016/0888-7543(90)90560-H

Genomics

Volume 6, Issue 2, February 1990, Pages 219-225

https://doi.org/10.1016/0888-7543(90)90560-H Get rights and content

Abstract

The genes for PGI (biglycan, BGN) and PGII (decorin, DCN) have been assigned to human chromosomes X and 12 by Southern analysis of a panel of human-rodent somatic cell hybrid DNAs with cDNA probes for these related small proteoglycans. Regional localization of BGN to Xq13-qter and DCN to 12q12.1-qter was also obtained by examining hybrids containing spontaneous breaks or well-characterized translocations involving chromosomes X and 12. Biglycan (BGN) is a single-copy gene about 6 kb in length. Hybridization with subfragment cDNA probes suggests the presence of two copies of the decorin (DCN) gene, or related sequences, at the locus on chromosome 12, although there is no evidence for function of more than one DCN gene. Efforts to detect restriction fragment length polymorphisms with these probes were unsuccessful.

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To investigate the pathophysiological role of macrophage-derived biglycan in HFHS diet-induced obesity, we generated chimeric mice in which biglycan is specifically deleted in myeloid cells. Since the Bgn gene is on the X chromosome (Chatterjee et al., 1993; McBride et al., 1990), male mice only have one copy. Thus, we chose to use male mice since it is easier to generate bone marrow-derived chimeric Bgn-deficient mice in males than females.
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Several studies have demonstrated a role for versican in pulmonary disorders and have been reviewed elsewhere [56]. Biglycan is a widely expressed proteoglycan that maps to the X chromosome [57]. It has an assembly role in the ECM, and disruption of the biglycan gene results in abnormal collagen fibril morphology [58].
The lung harbors a complex immune system composed of both innate and adaptive immune cells. Recognition of infection and injury by receptors on lung innate immune cells is crucial for generation of antigen-specific responses by adaptive immune cells. The extracellular matrix of the lung, comprising the interstitium and basement membrane, plays a key role in the regulation of these immune systems. The matrix consists of several hundred assembled proteins that interact to form a bioactive scaffold. This template, modified by enzymes, acts to facilitate cell function and differentiation and changes dynamically with age and lung disease. Herein, we explore relationships between innate and adaptive immunity and the lung extracellular matrix. We discuss the interactions between extracellular matrix proteins, including glycosaminoglycans, with prominent effects on innate immune signaling effectors such as toll-like receptors. We describe the relationship of extracellular matrix proteins with adaptive immunity and leukocyte migration to sites of injury within the lung. Further study of these interactions will lead to greater knowledge of the role of matrix biology in lung immunity. The development of novel therapies for acute and chronic lung disease is dependent on a comprehensive understanding of these complex matrix-immunity interactions.
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A literature search was performed and reviewed using the narrative approach.
As a class I SLRP member, asporin, is distinct from other SLRPs. Accumulating evidence demonstrates the involvement of asporin in OA pathogenesis. Many human studies have been conducted to explore the association between the D-repeat polymorphisms and OA susceptibility, but these yield inconsistent results. Possible mechanisms for the involvement of asporin in OA pathology include its influence on TGF-β (transforming growth factor-β) signaling pathways and collagen mineralization. To date, no studies were found to use an asporin-deficient animal model that would help to understand disease mechanisms. Many issues must be addressed to clarify the link between asporin and OA to provide a novel therapeutic strategy for OA, perhaps through controlling and modifying the TGF-β-ECM system.
Studies examined demonstrate the involvement of asporin in OA pathogenesis, and possible mechanisms by which asporin may be involved in this process have been proposed. However, large-scale interracial studies should be conducted to investigate the association between asporin and OA, and further investigations are needed to obtain a better understanding of the disease mechanism, develop novel therapeutic strategies, and explore new approaches for diagnosis of OA.
Bone Matrix and Mineralization
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This chapter provides an overview on the composition of the extracellular matrix of bone and discusses the matrix mineralization, and how proteins in the matrix are thought to regulate the process. The organic matrix constitutes approximately 20%—30% by weight of bone. The organic matrix contains approximately 90% collagen (by weight) and 10% non-collagenous proteins, proteoglycans, and lipids. Plasma proteins are also present in the organic matrix. Many plasma proteins permeate bone deriving from its rich vasculature, but have little or no affinity for bone, whereas others such as α₂-HS glycoprotein (fetuin A) have a higher affinity for the matrix and/or mineral of bone. The mineralization of vertebrate bone is a remarkable melding of geological and biological processes. The location of mineral within bone extracellular matrix clearly resides both within, and between, the collagen fibrils. These distinct ultra structural compartments for the mineral phase invariably provide different spatial and chemical environments for crystal growth, affecting crystal size and orientation. Beyond the initiation of mineralization in bone, crystal growth is regulated by a subcategory of the secreted, calcium-binding phosphoprotein (SCPP) family called the small, integrin-binding ligand, N-linked glycoproteins (SIBLINGs) that includes: OPN, MEPE, BSP, DMP1 and DSPP. The need for crystal growth inhibitors in tissues destined for mineralization may not at first glance be readily apparent but the massive mineralization events that occur in bones and teeth require a significant level of SIBLING protein regulation at the organic—inorganic interface as crystals must attain tissue-specific size, shape, and orientation with the extracellular matrix.
Bone Matrix and Mineralization
2011, Pediatric Bone: Biology and Diseases
This chapter provides an overview on the composition of the extracellular matrix of bone and discusses the matrix mineralization, and how proteins in the matrix are thought to regulate the process. The organic matrix constitutes approximately 20%—30% by weight of bone. The organic matrix contains approximately 90% collagen (by weight) and 10% non-collagenous proteins, proteoglycans, and lipids. Plasma proteins are also present in the organic matrix. Many plasma proteins permeate bone deriving from its rich vasculature, but have little or no affinity for bone, whereas others such as α₂-HS glycoprotein (fetuin A) have a higher affinity for the matrix and/or mineral of bone. The mineralization of vertebrate bone is a remarkable melding of geological and biological processes. The location of mineral within bone extracellular matrix clearly resides both within, and between, the collagen fibrils. These distinct ultra structural compartments for the mineral phase invariably provide different spatial and chemical environments for crystal growth, affecting crystal size and orientation. Beyond the initiation of mineralization in bone, crystal growth is regulated by a subcategory of the secreted, calcium-binding phosphoprotein (SCPP) family called the small, integrin-binding ligand, N-linked glycoproteins (SIBLINGs) that includes: OPN, MEPE, BSP, DMP1 and DSPP. The need for crystal growth inhibitors in tissues destined for mineralization may not at first glance be readily apparent but the massive mineralization events that occur in bones and teeth require a significant level of SIBLING protein regulation at the organic—inorganic interface as crystals must attain tissue-specific size, shape, and orientation with the extracellular matrix.
Proteoglycans of the Intervertebral Disk
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The intervertebral disks are fibrocartilages that separate the vertebrae of the spine and permit the twisting and bending associated with spine mobility. They also provide the resistance to compression required for the spines of bipeds to counteract the force of gravity. At first sight, the intervertebral disks seem ill equipped to deal with the constant mechanical insults to which they are exposed during daily life. They have no vascular system to provide the nutrients needed for cell metabolism, and are only sparsely populated with cells that are required to maintain the integrity of regions of the tissue that may be very remote. The solution to these problems resides in the unique structure of the extracellular matrix, which facilitates normal disk function and protects the cells from injury by mechanical trauma. The disks are composed of two regions that are structurally and functionally distinct—the outer annulus fibrosus (AF) and the central nucleus pulposus (NP). The AF consists of concentric lamellae rich in collagen, whereas the NP has a more gelatinous texture due to its lower collagen content and a high abundance of proteoglycan. The intervertebral disk proteoglycans are essential for normal tissue organization and metabolism, and perturbation in their abundance or structure can have dire consequences on tissue formation in the embryo, growth in the juvenile, and function in the adult. In the adult, detrimental changes in proteoglycan content and structure are associated with disk degeneration.

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^☆: Sequence data from this article have been deposited with the EMBL/GenBank Data Libraries under Accession No. JO4599.

^☆☆: PGI (biglycan) and PGII (decorin) have been assigned the symbols BGN and DCN, respectively, by the Human Gene Nomenclature Committee.

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Localization of PGI (biglycan, BGN) and PGII (decorin, DCN, PG-40) genes on human chromosomes Xq13-qter and 12q, respectively☆,☆☆

Abstract

Birth Defects Orig. Artic. Ser

Molecular cloning and sequence analysis of the cDNA for small proteoglycan II of bovine bone

Biochem. J

Identification of human RNA transcripts among heterogeneous nuclear RNA from man-mouse somatic cell hybrids

Deduced-protein sequence of bone small proteoglycan I (biglycan) shows homology with proteoglycan II (decorin) and several nonconnective tissue proteins in a variety of species

J. Biol. Chem

Localization of human gene loci using spontaneous chromosome rearrangements in human-Chinese hamster somatic cell hybrids

Amer. J. Hum. Genet

Proteoglycan core protein families

Annu. Rev. Biochem

The core proteins of large and small interstitial proteoglycans from various connective tissues form distinct subgroups

Biochem. J

Primary structure of an extracellular matrix proteoglycan core protein deduced from cloned cDNA

Fibronectin-mediated adhesion of fibroblasts: Inhibition by dermatan sulfate proteoglycan and evidence for a cryptic glycosaminoglycan-binding domain

J. Cell Biol

Chromosomal location of human kappa and lambda immunoglobulin light chain constant region genes

J. Exp. Med

Localization of human variable and constant region immunoglobulin heavy chain genes on subtelomeric band q32 of chromosome 14

Nucleic Acids Res