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muscle, protein, article, pparγ, skeletal, insulin, subjects, tissue, diabetes, privacy, cookies, ppars, adipose, content, information, publish, search, diabetologia, action, fat, type, diabetic, analysis, data, journal, research, distribution, peroxisome, proliferatoractivated, receptors, human, download, loviscach, rehman, carter, role, pparα, expression, glucose, disposal, rates, discover, optional, personal, parties, policy, find, track, relation, cite,

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peroxisome proliferator-activated receptors type ii diabetes privacy choices/manage cookies skeletal muscle pparγ human skeletal muscle muscle biopsy specimens impaired insulin action main content log type ii muscle pparγ protein european economic area statistically significant difference glucose disposal rates weight matched counterparts conditions privacy policy western blot analysis subgroup analysis showed muscle ppar skeletal muscle diabetes mellitus accepting optional cookies scope submit manuscript san diego catholic university nijmegen pparγ protein found search search journal finder publish pparγ protein expression insulin action related subjects muscle relative diabetes insulin-dependent pre-clamp insulin resistance article cite privacy policy personal data article loviscach henry department books a tissue distribution optional cookies manage preferences pparγ protein information protein expression diabetic subjects diabetic subjects usage analysis

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WebPage:
      mainEntity:
         headline:Distribution of peroxisome proliferator-activated receptors (PPARs) in human skeletal muscle and adipose tissue: relation to insulin action
         description: Aims/hypothesis. To evaluate the tissue distribution and possible role of the peroxisome proliferator-activated receptors (PPARs) in insulin action in fat and muscle biopsy specimens from lean, obese and subjects with Type II (non-insulin-dependent) diabetes mellitus.¶Methods. We measured PPARα, PPARβ(δ) and PPARγ protein expression by western blot analysis. The PPARγ protein was also measured in muscle before and after 3-h hyperinsulinaemic (300 mU · m–2· min–1) euglycaemic clamps.¶Results. The PPARα protein was expressed preferentially in muscle relative to fat (more than sevenfold). The PPARβ protein was similar in fat and muscle. The amount of PPARγ protein found in muscle was, on average, two-thirds of that present in fat. There was no statistically significant difference between non-diabetic and diabetic subjects in baseline (pre-clamp) muscle PPAR (α, β or γ) protein expression. Subgroup analysis showed, however, significantly higher PPARγ protein in the most insulin resistant diabetic subjects with glucose disposal rates of 3–6 mg · kg–1· min–1 compared with their age and weight matched counterparts with glucose disposal rates of 6–9 (147 ± 23 vs 88 ± 10 AU/μg protein, p≤ 0.01 in diabetic and vs 94 ± 15, p≤ 0.04 in non-diabetic subjects). Muscle PPARγ protein and glucose disposal rates were inversely correlated in diabetic subjects (r = –0.47, p≤ 0.05).¶Conclusion/interpretation. All PPARs (α, β or γ) are present in skeletal muscle and adipose tissue with different relative distributions. The PPARγ protein is abundant in skeletal muscle as well as adipose tissue. The altered expression of skeletal muscle PPARγ is consistent with a role for this nuclear protein in the impaired insulin action of Type II diabetes. [Diabetologia (2000) 43: 304–311]
         datePublished:
         dateModified:
         pageStart:304
         pageEnd:311
         sameAs:https://doi.org/10.1007/s001250050048
         keywords:
            Keywords Type II diabetes, insulin resistance, PPARα, PPARβ, PPARγ, protein, obesity, skeletal muscle, adipose tissue, human.
            Internal Medicine
            Metabolic Diseases
            Human Physiology
         image:
         isPartOf:
            name:Diabetologia
            issn:
               1432-0428
               0012-186X
            volumeNumber:43
            type:
               Periodical
               PublicationVolume
         publisher:
            name:Springer-Verlag
            logo:
               url:https://www.springernature.com/app-sn/public/images/logo-springernature.png
               type:ImageObject
            type:Organization
         author:
               name:M. Loviscach
               affiliation:
                     name:VA San Diego Healthcare System, San Diego, California, USA
                     address:
                        name:VA San Diego Healthcare System, San Diego, California, USA, , US
                        type:PostalAddress
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               name:N. Rehman
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                     name:VA San Diego Healthcare System, San Diego, California, USA
                     address:
                        name:VA San Diego Healthcare System, San Diego, California, USA, , US
                        type:PostalAddress
                     type:Organization
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               name:L. Carter
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                     name:VA San Diego Healthcare System, San Diego, California, USA
                     address:
                        name:VA San Diego Healthcare System, San Diego, California, USA, , US
                        type:PostalAddress
                     type:Organization
               type:Person
               name:S. Mudaliar
               affiliation:
                     name:VA San Diego Healthcare System, San Diego, California, USA
                     address:
                        name:VA San Diego Healthcare System, San Diego, California, USA, , US
                        type:PostalAddress
                     type:Organization
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               name:P. Mohadeen
               affiliation:
                     name:VA San Diego Healthcare System, San Diego, California, USA
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                        name:VA San Diego Healthcare System, San Diego, California, USA, , US
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                        name:VA San Diego Healthcare System, San Diego, California, USA, , US
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               name:J. H. Veerkamp
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                     name:Department of Biochemistry, Catholic University Nijmegen, Nijmegen, The Netherlands
                     address:
                        name:Department of Biochemistry, Catholic University Nijmegen, Nijmegen, The Netherlands, , NL
                        type:PostalAddress
                     type:Organization
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               name:R. R. Henry
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                     name:VA San Diego Healthcare System, San Diego, California, USA
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                        name:VA San Diego Healthcare System, San Diego, California, USA, , US
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         isAccessibleForFree:1
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      context:https://schema.org
ScholarlyArticle:
      headline:Distribution of peroxisome proliferator-activated receptors (PPARs) in human skeletal muscle and adipose tissue: relation to insulin action
      description: Aims/hypothesis. To evaluate the tissue distribution and possible role of the peroxisome proliferator-activated receptors (PPARs) in insulin action in fat and muscle biopsy specimens from lean, obese and subjects with Type II (non-insulin-dependent) diabetes mellitus.¶Methods. We measured PPARα, PPARβ(δ) and PPARγ protein expression by western blot analysis. The PPARγ protein was also measured in muscle before and after 3-h hyperinsulinaemic (300 mU · m–2· min–1) euglycaemic clamps.¶Results. The PPARα protein was expressed preferentially in muscle relative to fat (more than sevenfold). The PPARβ protein was similar in fat and muscle. The amount of PPARγ protein found in muscle was, on average, two-thirds of that present in fat. There was no statistically significant difference between non-diabetic and diabetic subjects in baseline (pre-clamp) muscle PPAR (α, β or γ) protein expression. Subgroup analysis showed, however, significantly higher PPARγ protein in the most insulin resistant diabetic subjects with glucose disposal rates of 3–6 mg · kg–1· min–1 compared with their age and weight matched counterparts with glucose disposal rates of 6–9 (147 ± 23 vs 88 ± 10 AU/μg protein, p≤ 0.01 in diabetic and vs 94 ± 15, p≤ 0.04 in non-diabetic subjects). Muscle PPARγ protein and glucose disposal rates were inversely correlated in diabetic subjects (r = –0.47, p≤ 0.05).¶Conclusion/interpretation. All PPARs (α, β or γ) are present in skeletal muscle and adipose tissue with different relative distributions. The PPARγ protein is abundant in skeletal muscle as well as adipose tissue. The altered expression of skeletal muscle PPARγ is consistent with a role for this nuclear protein in the impaired insulin action of Type II diabetes. [Diabetologia (2000) 43: 304–311]
      datePublished:
      dateModified:
      pageStart:304
      pageEnd:311
      sameAs:https://doi.org/10.1007/s001250050048
      keywords:
         Keywords Type II diabetes, insulin resistance, PPARα, PPARβ, PPARγ, protein, obesity, skeletal muscle, adipose tissue, human.
         Internal Medicine
         Metabolic Diseases
         Human Physiology
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      isPartOf:
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         issn:
            1432-0428
            0012-186X
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      author:
            name:M. Loviscach
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            name:N. Rehman
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            name:L. Carter
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                     name:VA San Diego Healthcare System, San Diego, California, USA, , US
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            name:T. P. Ciaraldi
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            name:J. H. Veerkamp
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                  name:Department of Biochemistry, Catholic University Nijmegen, Nijmegen, The Netherlands
                  address:
                     name:Department of Biochemistry, Catholic University Nijmegen, Nijmegen, The Netherlands, , NL
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            name:R. R. Henry
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