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Research article| Volume 119, ISSUE 1, P74-78, October 1993

Collagen fibril diameter and its relation to cross-linking of collagen in the skin of patients with amyotrophic lateral sclerosis

  • Seiitsu Ono
    Affiliations
    Department of Neurology, Teikyo University School of Medicine, Ichihara Hospital, Ichihara-City, Chiba, Japan
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  • Mitsuo Yamauchi
    Correspondence
    Correspondence to: Mitsuo Yamauchi, Dental Research Center, CB #7455, the University of North Carolina at Chapel Hill, Chapel Hill, NC 27599-7455, U.S.A., Tel: 919-966-5274; Fax: 919-966-1231
    Affiliations
    Dental Research Center, CB #7455, The University of North Carolina at Chapel Hill, Chapel Hill, NC, USA
    Search for articles by this author
DOI:https://doi.org/10.1016/0022-510X(93)90193-3
Collagen fibril diameter and its relation to cross-linking of collagen in the skin of patients with amyotrophic lateral sclerosis
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      Abstract

      The diameter of collagen fibrils and the age-related, stable cross-link, histidinohydroxylysinonorleucine (HHL), of skin tissue (left biceps) were measured and compared in 11 patients with amyotrophic lateral sclerosis (ALS) and 7 controls. In ALS patients, it was found that (1) the diameter of collagen fibrils and the content of HHL were negatively and significantly associated with the duration of illness (r = −0.74, P < 0.01 and r = −0.72, P < 0.02, respectively), and (2) there was an appreciable positive correlation between the diameter of collagen fibrils and the content of HHL (r = 0.73, P < 0.02). These findings were not observed in controls. These suggest there is a close relationship between the decreased amount of HHL and the small diameter of collagen fibrils in ALS.

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      References

        • Beach R.L.
        • Rao J.S.
        • Festoff B.W.
        • Reyes E.T.
        • Yanagihara R.
        • Gajusek D.C.
        Collagenase activity in skin fibroblasts of patients with amyotrophic lateral sclerosis.
        J. Neurol. Sci. 1986; 72: 49-60
        • Birk D.E.
        • Lande M.A.
        Corneal and scleral collagen fiber formation in vitro.
        Biochim. Biophys. Acta. 1981; 670: 362-369
        • Buck R.C.
        Collagen fibril diameter in the common carotid artery of the rat.
        Connect. Tissue Res. 1987; 16: 121-129
        • Cintron C.
        • Hassinger L.C.
        • Kublin C.L.
        • Cannon D.J.
        Biochemical and ultrastructural changes in collagen during corneal wound healing.
        J. Ultrastruct. Res. 1978; 65: 13-22
        • Epstein Jr., E.H.
        [α1(III)]3 human skin collagen: release by pepsin digestion and preponderance in fetal life.
        J. Biol. Chem. 1974; 249: 3225-3231
        • Fleischmajer R.
        • Olsen B.R.
        • Timpl R.
        • Perlish J.S.
        • Lovelace O.
        Collagen fibril formation during embryogenesis.
        in: Proc. Natl. Acad. Sci. USA. 80. 1983: 3354-3358
        • Flint M.H.
        • Craig A.S.
        • Reilly H.C.
        • Gillard G.C.
        • Parry D.A.D.
        Collagen fibril diameters and glycosaminoglycan content of skins - indices of tissue maturity and function.
        Connect. Tissue Res. 1984; 13: 69-81
        • Forrest L.
        • Dixon J.
        • Jackson D.S.
        Comparative studies on the insoluble collagens of guinea-pig dermis and dermal scar tissue.
        Connect. Tissue Res. 1972; 1: 243-250
        • Fullmer H.M.
        • Siedler H.D.
        • Krooth R.S.
        • Kurland L.T.
        A cutaneous disorder of connective tissue in amyotrophic lateral sclerosis: a histochemical study.
        Neurology. 1960; 10: 717-724
        • Gabella G.
        The collagen fibrils in the collapsed and the chronically stretched intestinal wall.
        J. Ultrastruct. Res. 1983; 85: 127-138
        • Greenlee T.K.
        • Pike D.
        Studies of tendon healing in the rat: remodeling of the distal stump after severance.
        Plast. Reconstr. Surg. 1971; 48: 260-270
        • Hama H.
        • Yamamoto T.
        • Takeda T.
        Experimental studies of connective tissue of the capsular ligament: influence of aging and sex hormones.
        Acta Orthop. Scand. 1976; 47: 473-479
        • Lapiere C.M.
        • Nusgens B.
        • Pierard G.E.
        Interaction between collagen type I and type III in conditioning bundles organization.
        Connect. Tissue Res. 1977; 5: 21-29
        • Mechanic G.L.
        • Katz E.P.
        • Henmi M.
        • Noyes C.
        • Yamauchi M.
        Locus of a histidine-based, stable trifunctional, helix to helix collagen cross-link: stereospecific collagen structure of type I skin fibrils.
        Biochemistry. 1987; 26: 3500-3509
        • Merrilees M.J.
        • Flint M.H.
        Ultrastructural study of tension and pressure zones in a rabbit flexor tendon.
        Am. J. Anat. 1980; 157: 87-106
        • Nimni M.E.
        • Harkness R.D.
        Molecular structures and functions of collagen.
        in: Nimni M.E. Collagen. CRC Press, Boca Raton, FL1988: 1-77
        • Ono S.
        • Toyokura Y.
        • Mannen T.
        • Ishibashi Y.
        Amyotrophic lateral sclerosis: histologic, histochemical, and ultrastructural abnormalities of skin.
        Neurology. 1986; 36: 948-956
        • Ono S.
        • Toyokura Y.
        • Mannen T.
        • Ishibashi Y.
        “Delayed return phenomenon” in amyotrophic lateral sclerosis.
        Acta Neurol. Scand. 1988; 77: 102-107
        • Ono S.
        • Toyokura Y.
        • Mannen T.
        • Ishibashi Y.
        Increased dermal collagen density in amyotrophic lateral sclerosis.
        J. Neurol. Sci. 1988; 83: 81-92
        • Ono S.
        • Mannen T.
        • Toyokura Y.
        Differential diagnosis between amyotrophic lateral sclerosis and spinal muscular atrophy by skin involvement.
        J. Neurol. Sci. 1989; 91: 301-310
        • Ono S.
        • Mechanic G.L.
        • Yamauchi M.
        Amyotrophic lateral sclerosis: unusually low content of collagen of skin.
        J. Neurol. Sci. 1990; 100: 234-237
        • Ono S.
        • Yamauchi M.
        Collagen cross-linking of skin in patients with amyotrophic lateral sclerosis.
        Ann. Neurol. 1992; 31: 305-310
        • Parry D.A.D.
        • Barnes G.R.G.
        • Craig A.S.
        A comparison of the size distribution of collagen fibrils in connective tissue as a function of age and a possible relation between fibril size distribution and mechanical properties.
        in: Proc. R. Soc. Lond. Ser. B. 203. 1978: 305-321
        • Scott J.E.
        • Orford C.R.
        Dermatan sulphate-rich proteoglycan associates with rat tail-tendon collagen at the d band in the gap region.
        Biochem. J. 1981; 197: 213-216
        • Stricklin G.P.
        • Hibbs M.S.
        Biochemistry and physiology of mammalian collagenases.
        in: Nimni M.E. Collagen. CRC Press, Boca Raton, FL1988: 187-205
        • Svoboda E.L.A.
        • Howley T.P.
        • Deporter D.A.
        Collagen fibril diameter and its relation to collagen turnover in three soft connective tissues in the rat.
        Connect. Tissue Res. 1983; 12: 43-48
        • Yamauchi M.
        • Noyes C.
        • Kuboki Y.
        • Mechanic G.L.
        Collagen structural microheterogeneity and a possible role for glycosylated hydroxylysine in type I collagen.
        in: Proc. Natl. Acad. Sci. USA. 79. 1982: 7684-7688
        • Yamauchi M.
        • London R.E.
        • Guenat C.
        • Hashimoto F.
        • Mechanic G.L.
        Structure and formation of a stable histidine-based trifunctional cross-link in skin collagen.
        J. Biol. Chem. 1987; 262: 11428-11434
        • Yamauchi M.
        • Mechanic G.L.
        Cross-linking of collagen.
        in: Nimni M.E. Collagen. CRC Press, Broca Raton, FL1988: 157-172
        • Yamauchi M.
        • Woodley D.T.
        • Mechanic G.L.
        Aging and cross-linking of skin collagen.
        Biochem. Biophys. Res. Commun. 1988; 152: 898-903
        • Yamauchi M.
        • Prisayanh P.
        • Haque Z.
        • Woodley D.T.
        Collagen cross-linking in sun-exposed and unexposed sites of aged human skin.
        J. Invest. Dermatol. 1991; 97: 938-941

      Article info

      Publication history

      Accepted: March 18, 1993
      Received in revised form: March 12, 1993
      Received: August 10, 1992

      Identification

      DOI: https://doi.org/10.1016/0022-510X(93)90193-3

      Copyright

      © 1993 Published by Elsevier Inc.

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