We are analyzing https://link.springer.com/article/10.1007/s00018-005-5410-y.

Title:
Anaplerotic roles of pyruvate carboxylase in mammalian tissues | Cellular and Molecular Life Sciences
Description:
Pyruvate carboxylase (PC) catalyzes the ATP-dependent carboxylation of pyruvate to oxaloacetate. PC serves an anaplerotic role for the tricarboxylic acid cycle, when intermediates are removed for different biosynthetic purposes. In liver and kidney, PC provides oxaloacetate for gluconeogenesis. In adipocytes PC is involved in de novo fatty acid synthesis and glyceroneogenesis, and is regulated by the peroxisome proliferator-activated receptor-γ, suggesting that PC is involved in the metabolic switch controlling fuel partitioning toward lipogenesis. In islets, PC is necessary for glucose-induced insulin secretion by providing oxaloacetate to form malate that participates in the ‘pyruvate/malate cycle’ to shuttle 3C or 4C between mitochondria and cytoplasm. Hyperglycemia and hyperlipidemia impair this cycle and affect glucose-stimulated insulin release. In astrocytes, PC is important for de novo synthesis of glutamate, an important excitatory neurotransmitter supplied to neurons. Transcriptional studies of the PC gene pinpoint some transcription factors that determine tissue-specific expression.
Website Age:
28 years and 1 months (reg. 1997-05-29).

Matching Content Categories {📚}

Telecommunications
Education
Science

Content Management System {📝}

What CMS is link.springer.com built with?

Custom-built

No common CMS systems were detected on Link.springer.com, and no known web development framework was identified.

Traffic Estimate {📈}

What is the average monthly size of link.springer.com audience?

🌠 Phenomenal Traffic: 5M - 10M visitors per month

Based on our best estimate, this website will receive around 7,734,772 visitors per month in the current month.

check SE Ranking
check Ahrefs
check Similarweb
check Ubersuggest
check Semrush

How Does Link.springer.com Make Money? {💸}

We can't tell how the site generates income.

Not every website is profit-driven; some are created to spread information or serve as an online presence. Websites can be made for many reasons. This could be one of them. Link.springer.com has a secret sauce for making money, but we can't detect it yet.

Keywords {🔍}

article, pyruvate, carboxylase, privacy, cookies, content, access, information, publish, search, jitrapakdee, biochemistry, data, log, journal, research, molecular, life, anaplerotic, roles, vidalpuig, wallace, oxaloacetate, cycle, synthesis, insulin, shuttle, discover, author, university, springer, optional, personal, parties, policy, find, track, cellular, sciences, cmls, mammalian, tissues, published, february, cite, explore, acid, involved, novo, glyceroneogenesis,

Topics {✒️}

glucose-induced insulin secretion peroxisome proliferator-activated receptor-γ �pyruvate/malate cycle de novo synthesis shuttle 3c month download article/chapter determine tissue-specific expression pyruvate carboxylase glyceroneogenesis lipogenesis astrocytes glutamate diabetes privacy choices/manage cookies form malate full article pdf check access instant access tricarboxylic acid cycle european economic area scope submit manuscript atp-dependent carboxylation mechanistic biological marker anaplerotic roles clinical biochemistry conditions privacy policy accepting optional cookies related subjects author correspondence pyruvate vidal-puig school pc gene pinpoint article cellular journal finder publish biochemistry life sci article log mammalian tissues privacy policy personal data anaplerotic role books a article cite article jitrapakdee optional cookies manage preferences subscription content similar content vidal-puig vidal-puig

Schema {🗺️}

WebPage:
      mainEntity:
         headline:Anaplerotic roles of pyruvate carboxylase in mammalian tissues
         description:Pyruvate carboxylase (PC) catalyzes the ATP-dependent carboxylation of pyruvate to oxaloacetate. PC serves an anaplerotic role for the tricarboxylic acid cycle, when intermediates are removed for different biosynthetic purposes. In liver and kidney, PC provides oxaloacetate for gluconeogenesis. In adipocytes PC is involved in de novo fatty acid synthesis and glyceroneogenesis, and is regulated by the peroxisome proliferator-activated receptor-γ, suggesting that PC is involved in the metabolic switch controlling fuel partitioning toward lipogenesis. In islets, PC is necessary for glucose-induced insulin secretion by providing oxaloacetate to form malate that participates in the ‘pyruvate/malate cycle’ to shuttle 3C or 4C between mitochondria and cytoplasm. Hyperglycemia and hyperlipidemia impair this cycle and affect glucose-stimulated insulin release. In astrocytes, PC is important for de novo synthesis of glutamate, an important excitatory neurotransmitter supplied to neurons. Transcriptional studies of the PC gene pinpoint some transcription factors that determine tissue-specific expression.
         datePublished:2006-02-28T00:00:00Z
         dateModified:2006-02-28T00:00:00Z
         pageStart:843
         pageEnd:854
         sameAs:https://doi.org/10.1007/s00018-005-5410-y
         keywords:
            Pyruvate carboxylase
            biotin carboxylase
            glucose-induced insulin secretion
            pyruvate/malate shuttle
            pyruvate/citrate shuttle
            type 2 diabetes
            lipogenesis
            glyceroneogenesis
            astrocytes
            glutamate synthesis
            Cell Biology
            Biomedicine
            general
            Life Sciences
            Biochemistry
         image:
         isPartOf:
            name:Cellular and Molecular Life Sciences CMLS
            issn:
               1420-9071
               1420-682X
            volumeNumber:63
            type:
               Periodical
               PublicationVolume
         publisher:
            name:Birkhäuser-Verlag
            logo:
               url:https://www.springernature.com/app-sn/public/images/logo-springernature.png
               type:ImageObject
            type:Organization
         author:
               name:S. Jitrapakdee
               affiliation:
                     name:Mahidol University
                     address:
                        name:Department of Biochemistry, Faculty of Science, Mahidol University, Bangkok, Thailand
                        type:PostalAddress
                     type:Organization
               email:[email protected]
               type:Person
               name:A. Vidal-Puig
               affiliation:
                     name:University of Cambridge
                     address:
                        name:Department of Clinical Biochemistry, University of Cambridge, Cambridge, United Kingdom
                        type:PostalAddress
                     type:Organization
               type:Person
               name:J. C. Wallace
               affiliation:
                     name:University of Adelaide
                     address:
                        name:School of Molecular and Biomedical Science, University of Adelaide, Adelaide, Australia
                        type:PostalAddress
                     type:Organization
               type:Person
         isAccessibleForFree:
         hasPart:
            isAccessibleForFree:
            cssSelector:.main-content
            type:WebPageElement
         type:ScholarlyArticle
      context:https://schema.org
ScholarlyArticle:
      headline:Anaplerotic roles of pyruvate carboxylase in mammalian tissues
      description:Pyruvate carboxylase (PC) catalyzes the ATP-dependent carboxylation of pyruvate to oxaloacetate. PC serves an anaplerotic role for the tricarboxylic acid cycle, when intermediates are removed for different biosynthetic purposes. In liver and kidney, PC provides oxaloacetate for gluconeogenesis. In adipocytes PC is involved in de novo fatty acid synthesis and glyceroneogenesis, and is regulated by the peroxisome proliferator-activated receptor-γ, suggesting that PC is involved in the metabolic switch controlling fuel partitioning toward lipogenesis. In islets, PC is necessary for glucose-induced insulin secretion by providing oxaloacetate to form malate that participates in the ‘pyruvate/malate cycle’ to shuttle 3C or 4C between mitochondria and cytoplasm. Hyperglycemia and hyperlipidemia impair this cycle and affect glucose-stimulated insulin release. In astrocytes, PC is important for de novo synthesis of glutamate, an important excitatory neurotransmitter supplied to neurons. Transcriptional studies of the PC gene pinpoint some transcription factors that determine tissue-specific expression.
      datePublished:2006-02-28T00:00:00Z
      dateModified:2006-02-28T00:00:00Z
      pageStart:843
      pageEnd:854
      sameAs:https://doi.org/10.1007/s00018-005-5410-y
      keywords:
         Pyruvate carboxylase
         biotin carboxylase
         glucose-induced insulin secretion
         pyruvate/malate shuttle
         pyruvate/citrate shuttle
         type 2 diabetes
         lipogenesis
         glyceroneogenesis
         astrocytes
         glutamate synthesis
         Cell Biology
         Biomedicine
         general
         Life Sciences
         Biochemistry
      image:
      isPartOf:
         name:Cellular and Molecular Life Sciences CMLS
         issn:
            1420-9071
            1420-682X
         volumeNumber:63
         type:
            Periodical
            PublicationVolume
      publisher:
         name:Birkhäuser-Verlag
         logo:
            url:https://www.springernature.com/app-sn/public/images/logo-springernature.png
            type:ImageObject
         type:Organization
      author:
            name:S. Jitrapakdee
            affiliation:
                  name:Mahidol University
                  address:
                     name:Department of Biochemistry, Faculty of Science, Mahidol University, Bangkok, Thailand
                     type:PostalAddress
                  type:Organization
            email:[email protected]
            type:Person
            name:A. Vidal-Puig
            affiliation:
                  name:University of Cambridge
                  address:
                     name:Department of Clinical Biochemistry, University of Cambridge, Cambridge, United Kingdom
                     type:PostalAddress
                  type:Organization
            type:Person
            name:J. C. Wallace
            affiliation:
                  name:University of Adelaide
                  address:
                     name:School of Molecular and Biomedical Science, University of Adelaide, Adelaide, Australia
                     type:PostalAddress
                  type:Organization
            type:Person
      isAccessibleForFree:
      hasPart:
         isAccessibleForFree:
         cssSelector:.main-content
         type:WebPageElement
["Periodical","PublicationVolume"]:
      name:Cellular and Molecular Life Sciences CMLS
      issn:
         1420-9071
         1420-682X
      volumeNumber:63
Organization:
      name:Birkhäuser-Verlag
      logo:
         url:https://www.springernature.com/app-sn/public/images/logo-springernature.png
         type:ImageObject
      name:Mahidol University
      address:
         name:Department of Biochemistry, Faculty of Science, Mahidol University, Bangkok, Thailand
         type:PostalAddress
      name:University of Cambridge
      address:
         name:Department of Clinical Biochemistry, University of Cambridge, Cambridge, United Kingdom
         type:PostalAddress
      name:University of Adelaide
      address:
         name:School of Molecular and Biomedical Science, University of Adelaide, Adelaide, Australia
         type:PostalAddress
ImageObject:
      url:https://www.springernature.com/app-sn/public/images/logo-springernature.png
Person:
      name:S. Jitrapakdee
      affiliation:
            name:Mahidol University
            address:
               name:Department of Biochemistry, Faculty of Science, Mahidol University, Bangkok, Thailand
               type:PostalAddress
            type:Organization
      email:[email protected]
      name:A. Vidal-Puig
      affiliation:
            name:University of Cambridge
            address:
               name:Department of Clinical Biochemistry, University of Cambridge, Cambridge, United Kingdom
               type:PostalAddress
            type:Organization
      name:J. C. Wallace
      affiliation:
            name:University of Adelaide
            address:
               name:School of Molecular and Biomedical Science, University of Adelaide, Adelaide, Australia
               type:PostalAddress
            type:Organization
PostalAddress:
      name:Department of Biochemistry, Faculty of Science, Mahidol University, Bangkok, Thailand
      name:Department of Clinical Biochemistry, University of Cambridge, Cambridge, United Kingdom
      name:School of Molecular and Biomedical Science, University of Adelaide, Adelaide, Australia
WebPageElement:
      isAccessibleForFree:
      cssSelector:.main-content

External Links {🔗}(29)

Analytics and Tracking {📊}

Google Tag Manager

Libraries {📚}

Clipboard.js
Prism.js

CDN Services {📦}

Crossref

4.01s.

LINK . SPRINGER . COM {}