Age Differences in Human Skin Collagen

1993 ◽  
pp. 278-282
Author(s):  
J. Brinckmann ◽  
M. Brey ◽  
P. K. Müller
Keyword(s):  
Human Skin ◽  
Age Differences ◽  
Skin Collagen

Age-dependent accumulation of N.epsilon.-(carboxymethyl)lysine and N.epsilon.-(carboxymethyl)hydroxylysine in human skin collagen

Biochemistry ◽  
1991 ◽  
Vol 30 (5) ◽  
pp. 1205-1210 ◽  
Author(s):  
John A. Dunn ◽  
David R. McCance ◽  
Suzanne R. Thorpe ◽  
Timothy J. Lyons ◽  
John W. Baynes
Keyword(s):  
Human Skin ◽  
Skin Collagen ◽  
Age Dependent ◽  
Carboxymethyl Lysine

Analysis of the age-related composition of human skin collagen and collagens synthesized by fibroblast culture

1994 ◽  
Vol 286 (7) ◽  
pp. 391-395 ◽  
Author(s):  
J. Brinckmann ◽  
M. Bodo ◽  
M. Brey ◽  
H. H. Wolff ◽  
P. K. M�ller
Keyword(s):  
Human Skin ◽  
Fibroblast Culture ◽  
Age Related ◽  
Skin Collagen

scholarly journals Modulation of Skin Collagen Metabolism in Aged and Photoaged Human Skin In Vivo

2001 ◽  
Vol 117 (5) ◽  
pp. 1218-1224 ◽  
Author(s):  
Jin Ho Chung ◽  
Jin Young Seo ◽  
Hai Ryung Choi ◽  
Mi Kyung Lee ◽  
Choon Shik Youn ◽  
...  
Keyword(s):  
Human Skin ◽  
Collagen Metabolism ◽  
Skin Collagen

scholarly journals THE STRUCTURE OF HUMAN SKIN COLLAGEN AS STUDIED WITH THE ELECTRON MICROSCOPE

1948 ◽  
Vol 88 (5) ◽  
pp. 555-568 ◽  
Author(s):  
Jerome Gross ◽  
Francis O. Schmitt
Keyword(s):  
Electron Microscope ◽  
Human Skin ◽  
Amorphous Material ◽  
Collagen Fibrils ◽  
Biopsy Material ◽  
Normal Human Skin ◽  
Skin Collagen ◽  
Aged Skin ◽  
Normal Human ◽  
Adult Skin

1. The structure of the collagen fibrils of normal human skin corium has been investigated with the electron microscope. 2. Under the conditions of observation the fibrils ranged in width from about 700 to 1,400 A with 1,000 A as the value occurring most frequently. They showed little tendency to fray longitudinally as is characteristic of tendon fibrils; when fracture of fibrils occurred it was usually in planes transverse to the axis. 3. The axial repeating periods observed in fibrils stained with phosphotungstic acid or shadowed with chromium or platinum range from about 500 to 800 A, the maximum occurring between 620 and 660 A. The average period in fibrils from infant skin does not differ significantly from that of adult and aged skin. 4. Depending on conditions of preparation, intraperiod fine structure, in the form of cross-bands, was observed in varying detail. The most detailed pattern commonly observed contains six bands of characteristic density and position. 5. Shadowed plastic replicas of dried collagen fibrils reproduce much of the structure commonly seen in shadowed fibrils. Replicas of moist fibrils show considerably less surface contouring than do dried fibrils. Replicas from smears of connective tissue fragments on glass show detailed structure, indicating the feasibility of applying this technique to biopsy material. 6. Infant skin differs from adult skin in having considerably greater amounts of amorphous material, little of which is strongly adherent to the collagen fibrils.

Titration of Human Skin Collagen Extracted with Acid*

Biochemistry ◽  
1966 ◽  
Vol 5 (11) ◽  
pp. 3488-3493 ◽  
Author(s):  
Seymour Bakerman ◽  
Boyd K. Hartman
Keyword(s):  
Human Skin ◽  
Skin Collagen
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