Macromolecular Evolution of Connective Tissue

Mathews, Martin B.

doi:10.1111/j.1469-185x.1967.tb01528.x

Cited by 107 publications

(15 citation statements)

References 266 publications

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“…The age-related decrease in the ratio of parenchymal chondroitin 4-sulfate to chondroitin 6-sulfate is in contrast to rabbit cartilage, in which this ratio increases with age (36). In human costal and tracheobronchial cartilage this ratio decreases with age (34,36 into GAG for at least 10 h (Fig. 3).…”

Section: Resultsmentioning

confidence: 85%

Content and synthesis of glycosaminoglycans in the developing lung.

Horwitz¹,

Crystal²

1975

J. Clin. Invest.

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A B S T R A C T The function of lung is fundamentally linked to the connective tissue composition of the alveolar interstitium. The composition and synthesis of one class of interstitial connective tissue components, the glycosaminoglycans (GAG), was determined in lung parenchyma of rabbits at different stages of development. Parenchymal GAG content ranged between 0.2 and 0.4% (wt/wt) of dry weight, with highest concentration in adult lung. There were significant changes in types of GAG present at different ages. Fetal lungs contained a relatively high proportion of chondroitin 4-sulfate while the GAG in lung parenchyma of older animals was predominantly dermatan sulfate, heparan sulfate, and heparin. Methods were developed for the study of rates of synthesis of GAG by incorporation of [1-'4C]glucosamine into lung explants. The rate of synthesis of total GAG per cell increased with development to a maximum in lung from weanling rabbits and fell to low rates of synthesis in mature rabbits. Fetal rabbit lung parenchyma synthesized mostly hyaluronic acid and heparan sulfate, while in weanling rabbit parenchyma hyaluronic acid and chondroitin 4/6-sulfate synthesis was greatest. In mature animals, the rates of synthesis of all types of GAG were relatively low structure, determination of lung mechanical properties, interchange of nutrients and metabolites between the capillary and epithelial cells, and diffusion of 02 and C02 between the alveolar gas and the blood. The two major constituents of interstitial connective tissue, collagen and elastin, comprise more than 90% of the noncellular interstitial dry weight. The remainder has been termed the "amorphous ground substance" (1, 2).The term "amorphous" is used because this material is poorly defined morphologically. It is known to include serum proteins, glycoproteins, cellular metabolites, small solutes (,e.g., glucose, urea, salts), and proteoglycans (3). The latter are macromolecules composed of a protein backbone with multiple, large polysaccharide side chains termed glycosaminoglycans (GAG) 1 (4). The GAG also include hyaluronic acid, which may not be part of a protein-polysaccharide complex. In tissues other than lung and in simplified model systems with purified components, it has been shown that specific types of GAG will: (a) associate with other connective tissue elements (5, 6); (b) influence the rate of synthesis of connective tissue components (7, 8); (c) affect the hydration of connective tissue (9); and (d) influence the rate of collagen fibril formation and subsequent stability of these fibrils (5, 10). Thus, the quantity and type of GAG in the lung interstitium may have significant effects on the mechanical properties of the lung as well as on gas, solute, and fluid movements between the alveolar space and capillary (11). It is the purpose of this study to describe methods to quantitate the composition and synthesis of GAG in the lung interstitium and to define the normal pattern of GAG accumulation and synthesis in the growing lung. METHODSMaterial...

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Section: Resultsmentioning

confidence: 85%

Content and synthesis of glycosaminoglycans in the developing lung.

Horwitz¹,

Crystal²

1975

J. Clin. Invest.

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“…Although chemical analysis of the glycosaminoglycans present in the two types of hag-fish cartilages were not determined in this investigation, comparative biochemical studies by Mathews (1967Mathews ( , 1975 indicate that most of the glycosaminoglycans of hagfish cartilage proteoglycans have an unusual chemical structure. They are a type of chondroitin sulfate that contains galactosamine that is sulfated both at C4 and C6.…”

Section: Discussionmentioning

confidence: 94%

Cartilage in the atlantic hagfish, Myxine glutinosa

et al. 1984

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Light and electron microscopic observations and biochemical analysis of the lingual cartilages from the Atlantic hagfish, Myxine glutinosa, reveal two different types of cartilage, designated types 1 and 2, respectively. The anterior and medial lingual are type 1, while the posterior lingual cartilage is type 2. Chondrocytes in type 1 cartilage are similar to those found in other vertebrate cartilages. The presence within the Golgi elements of material that resembles a component of the extracellular matrix suggests the involvement of active chondrocytes in the synthesis of the matrix. The matrix of the type 1 cartilage contains fibrils arranged to form concentric lamellae in the territorial matrix and irregularly arranged, branched fibrils in the interterritorial matrix. Biochemical analysis of the type 1 cartilage reveals that it is composed primarily of a cyanogen bromide (CNBr)-insoluble protein of unique composition that we have termed " myxinin ." Myxinin appears to be similar, but not identical, to lamprin . Type 2 cartilage bears no resemblance to any other known vertebrate cartilage. The principal cells are hypertrophied and are characterized by masses of cytoplasmic filaments. The appearance of the organelles in smaller nest cells suggests that nest cells are active in the production of some of the matrix, which consists primarily of collagen. Microfibrils and a basal lamina-like material are also present. Biochemical analysis of the type 2 cartilage reveals that the CNBr-insoluble material is different from myxinin . Comparisons of lamprey and hagfish cartilages prompt the concept that these two agnathans probably followed long-independent evolutionary histories.

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“…The details of cartilage formation and development are dealt with in other chapters of this book and in other works, (Mathews, 1968;Hall, 1975;O'Rahilly and Gardner, 1978). Here we can treat only briefly a few salient points that will help us to have a better perspective on the mechanism of cartilage calcification.…”

Section: Introductionmentioning

confidence: 99%

Calcification of Cartilage

Ali¹

1983

Cartilage

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Macromolecular Evolution of Connective Tissue

Cited by 107 publications

References 266 publications

Content and synthesis of glycosaminoglycans in the developing lung.

Content and synthesis of glycosaminoglycans in the developing lung.

Cartilage in the atlantic hagfish, Myxine glutinosa

Calcification of Cartilage

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