Proline metabolism in cancer
Cancer cells often change their metabolism to support uncontrolled proliferation. Proline is the only proteogenic secondary amino acid that is abundant in the body. Recent studies have shown that proline metabolism plays an important role in metabolic reprogramming and affects the occurrence and dev...
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| Veröffentlicht in: | Amino acids 2021-12, Vol.53 (12), p.1769-1777 |
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| creator | Geng, Pengyu Qin, Wangshu Xu, Guowang |
| description | Cancer cells often change their metabolism to support uncontrolled proliferation. Proline is the only proteogenic secondary amino acid that is abundant in the body. Recent studies have shown that proline metabolism plays an important role in metabolic reprogramming and affects the occurrence and development of cancer. Proline metabolism is related to ATP production, protein and nucleotide synthesis, and redox homeostasis in tumor cells. Proline can be synthesized by aldehyde dehydrogenase family 18 member A1 (ALDH18A1) and delta1-pyrroline-5-carboxylate reductase (PYCR), up-regulating ALDH18A1 and PYCR can promote the proliferation and invasion of cancer cells. As the main storage of proline, collagen can influence cancer cells proliferation, invasion, and metastasis. Its synthesis depends on the hydroxylation of proline catalyzed by prolyl 4-hydroxylases (P4Hs), which will affect the plasticity and metastasis of cancer cells. The degradation of proline occurs in the mitochondria and involves an oxidation step catalyzed by proline dehydrogenase/proline oxidase (PRODH/POX). Proline catabolism has a dual role in cancer, linking apoptosis with the survival and metastasis of cancer cells. In addition, it has been demonstrated that the regulation of proline metabolic enzymes at the genetic and post-translational levels is related to cancer. This article reviews the role of proline metabolic enzymes in cancer proliferation, apoptosis, metastasis, and development. Research on proline metabolism may provide a new strategy for cancer treatment. |
| doi_str_mv | 10.1007/s00726-021-03060-1 |
| format | Article |
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Proline is the only proteogenic secondary amino acid that is abundant in the body. Recent studies have shown that proline metabolism plays an important role in metabolic reprogramming and affects the occurrence and development of cancer. Proline metabolism is related to ATP production, protein and nucleotide synthesis, and redox homeostasis in tumor cells. Proline can be synthesized by aldehyde dehydrogenase family 18 member A1 (ALDH18A1) and delta1-pyrroline-5-carboxylate reductase (PYCR), up-regulating ALDH18A1 and PYCR can promote the proliferation and invasion of cancer cells. As the main storage of proline, collagen can influence cancer cells proliferation, invasion, and metastasis. Its synthesis depends on the hydroxylation of proline catalyzed by prolyl 4-hydroxylases (P4Hs), which will affect the plasticity and metastasis of cancer cells. The degradation of proline occurs in the mitochondria and involves an oxidation step catalyzed by proline dehydrogenase/proline oxidase (PRODH/POX). Proline catabolism has a dual role in cancer, linking apoptosis with the survival and metastasis of cancer cells. In addition, it has been demonstrated that the regulation of proline metabolic enzymes at the genetic and post-translational levels is related to cancer. This article reviews the role of proline metabolic enzymes in cancer proliferation, apoptosis, metastasis, and development. Research on proline metabolism may provide a new strategy for cancer treatment.</description><identifier>ISSN: 0939-4451</identifier><identifier>EISSN: 1438-2199</identifier><identifier>DOI: 10.1007/s00726-021-03060-1</identifier><identifier>PMID: 34390414</identifier><language>eng</language><publisher>Vienna: Springer Vienna</publisher><subject>Adenosine triphosphate ; Aldehyde dehydrogenase ; Aldehydes ; Amino acids ; Analytical Chemistry ; Animals ; Apoptosis ; Apoptosis - physiology ; Biochemical Engineering ; Biochemistry ; Biomedical and Life Sciences ; Cancer ; Carboxylate reductase ; Catabolism ; Cell proliferation ; Cell Proliferation - physiology ; Collagen ; Dehydrogenases ; Enzymes ; Homeostasis ; Humans ; Hydroxylation ; Life Sciences ; Metabolism ; Metastases ; Metastasis ; Mitochondria ; Neoplasm Metastasis - pathology ; Neoplasms - metabolism ; Neoplasms - pathology ; Neurobiology ; Nucleotides ; Oxidation ; Post-translation ; Proline ; Proline - metabolism ; Proline dehydrogenase ; Proline metabolism in cancer ; Proline oxidase ; Protein biosynthesis ; Protein turnover ; Proteomics ; Pyrroline-5-carboxylate reductase ; Reductases ; Review Article ; Tumor cells</subject><ispartof>Amino acids, 2021-12, Vol.53 (12), p.1769-1777</ispartof><rights>The Author(s), under exclusive licence to Springer-Verlag GmbH Austria, part of Springer Nature 2021</rights><rights>2021. 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Proline is the only proteogenic secondary amino acid that is abundant in the body. Recent studies have shown that proline metabolism plays an important role in metabolic reprogramming and affects the occurrence and development of cancer. Proline metabolism is related to ATP production, protein and nucleotide synthesis, and redox homeostasis in tumor cells. Proline can be synthesized by aldehyde dehydrogenase family 18 member A1 (ALDH18A1) and delta1-pyrroline-5-carboxylate reductase (PYCR), up-regulating ALDH18A1 and PYCR can promote the proliferation and invasion of cancer cells. As the main storage of proline, collagen can influence cancer cells proliferation, invasion, and metastasis. Its synthesis depends on the hydroxylation of proline catalyzed by prolyl 4-hydroxylases (P4Hs), which will affect the plasticity and metastasis of cancer cells. The degradation of proline occurs in the mitochondria and involves an oxidation step catalyzed by proline dehydrogenase/proline oxidase (PRODH/POX). Proline catabolism has a dual role in cancer, linking apoptosis with the survival and metastasis of cancer cells. In addition, it has been demonstrated that the regulation of proline metabolic enzymes at the genetic and post-translational levels is related to cancer. This article reviews the role of proline metabolic enzymes in cancer proliferation, apoptosis, metastasis, and development. Research on proline metabolism may provide a new strategy for cancer treatment.</description><subject>Adenosine triphosphate</subject><subject>Aldehyde dehydrogenase</subject><subject>Aldehydes</subject><subject>Amino acids</subject><subject>Analytical Chemistry</subject><subject>Animals</subject><subject>Apoptosis</subject><subject>Apoptosis - physiology</subject><subject>Biochemical Engineering</subject><subject>Biochemistry</subject><subject>Biomedical and Life Sciences</subject><subject>Cancer</subject><subject>Carboxylate reductase</subject><subject>Catabolism</subject><subject>Cell proliferation</subject><subject>Cell Proliferation - physiology</subject><subject>Collagen</subject><subject>Dehydrogenases</subject><subject>Enzymes</subject><subject>Homeostasis</subject><subject>Humans</subject><subject>Hydroxylation</subject><subject>Life Sciences</subject><subject>Metabolism</subject><subject>Metastases</subject><subject>Metastasis</subject><subject>Mitochondria</subject><subject>Neoplasm Metastasis - pathology</subject><subject>Neoplasms - metabolism</subject><subject>Neoplasms - pathology</subject><subject>Neurobiology</subject><subject>Nucleotides</subject><subject>Oxidation</subject><subject>Post-translation</subject><subject>Proline</subject><subject>Proline - metabolism</subject><subject>Proline dehydrogenase</subject><subject>Proline metabolism in cancer</subject><subject>Proline oxidase</subject><subject>Protein biosynthesis</subject><subject>Protein turnover</subject><subject>Proteomics</subject><subject>Pyrroline-5-carboxylate reductase</subject><subject>Reductases</subject><subject>Review Article</subject><subject>Tumor cells</subject><issn>0939-4451</issn><issn>1438-2199</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2021</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>BENPR</sourceid><recordid>eNp9kMtKxDAUhoMozjj6AiIy4MZN9JxcmmYpgzcY0IWuQ5om0mHajsl04dsbrRdw4SYJ5Pv_c_gIOUa4QAB1mfLBCgoMKXAogOIOmaLgJWWo9S6ZguaaCiFxQg5SWgEgK7HYJxMuuAaBYkpOHmO_bjo_b_3WVvmZ2nnTzZ3tnI-HZC_YdfJHX_eMPN9cPy3u6PLh9n5xtaSOK7mllsmqFCXTUGulpAClhXW6lnUZZNCgHdiAtauCYzxIJwoFoWa-kEI4LD2fkfOxdxP718GnrWmb5Px6bTvfD8kwWaDQqLjK6NkfdNUPscvbGVaAytVa6UyxkXKxTyn6YDaxaW18Mwjmw50Z3Znszny6M5hDp1_VQ9X6-ifyLSsDfARS_upefPyd_U_tOzNDdpk</recordid><startdate>20211201</startdate><enddate>20211201</enddate><creator>Geng, Pengyu</creator><creator>Qin, Wangshu</creator><creator>Xu, Guowang</creator><general>Springer Vienna</general><general>Springer Nature B.V</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>3V.</scope><scope>7TK</scope><scope>7X7</scope><scope>7XB</scope><scope>88E</scope><scope>8AO</scope><scope>8FE</scope><scope>8FG</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>ABJCF</scope><scope>ABUWG</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BGLVJ</scope><scope>BHPHI</scope><scope>CCPQU</scope><scope>D1I</scope><scope>DWQXO</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>KB.</scope><scope>LK8</scope><scope>M0S</scope><scope>M1P</scope><scope>M7P</scope><scope>PDBOC</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PRINS</scope><scope>7X8</scope><orcidid>https://orcid.org/0000-0003-4298-3554</orcidid></search><sort><creationdate>20211201</creationdate><title>Proline metabolism in cancer</title><author>Geng, Pengyu ; Qin, Wangshu ; Xu, Guowang</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c375t-a25b848290d977540794ac9d5d8f5f909c0af1dcbfc23f5c4670fd2e6544c18e3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2021</creationdate><topic>Adenosine triphosphate</topic><topic>Aldehyde dehydrogenase</topic><topic>Aldehydes</topic><topic>Amino acids</topic><topic>Analytical Chemistry</topic><topic>Animals</topic><topic>Apoptosis</topic><topic>Apoptosis - physiology</topic><topic>Biochemical Engineering</topic><topic>Biochemistry</topic><topic>Biomedical and Life Sciences</topic><topic>Cancer</topic><topic>Carboxylate reductase</topic><topic>Catabolism</topic><topic>Cell proliferation</topic><topic>Cell Proliferation - physiology</topic><topic>Collagen</topic><topic>Dehydrogenases</topic><topic>Enzymes</topic><topic>Homeostasis</topic><topic>Humans</topic><topic>Hydroxylation</topic><topic>Life Sciences</topic><topic>Metabolism</topic><topic>Metastases</topic><topic>Metastasis</topic><topic>Mitochondria</topic><topic>Neoplasm Metastasis - pathology</topic><topic>Neoplasms - metabolism</topic><topic>Neoplasms - pathology</topic><topic>Neurobiology</topic><topic>Nucleotides</topic><topic>Oxidation</topic><topic>Post-translation</topic><topic>Proline</topic><topic>Proline - metabolism</topic><topic>Proline dehydrogenase</topic><topic>Proline metabolism in cancer</topic><topic>Proline oxidase</topic><topic>Protein biosynthesis</topic><topic>Protein turnover</topic><topic>Proteomics</topic><topic>Pyrroline-5-carboxylate reductase</topic><topic>Reductases</topic><topic>Review Article</topic><topic>Tumor cells</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Geng, Pengyu</creatorcontrib><creatorcontrib>Qin, Wangshu</creatorcontrib><creatorcontrib>Xu, Guowang</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>ProQuest Central (Corporate)</collection><collection>Neurosciences Abstracts</collection><collection>Health & Medical Collection</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Medical Database (Alumni Edition)</collection><collection>ProQuest Pharma Collection</collection><collection>ProQuest SciTech Collection</collection><collection>ProQuest Technology Collection</collection><collection>ProQuest Natural Science Collection</collection><collection>Hospital Premium Collection</collection><collection>Hospital Premium Collection (Alumni Edition)</collection><collection>ProQuest Central (Alumni) (purchase pre-March 2016)</collection><collection>Materials Science & Engineering Collection</collection><collection>ProQuest Central (Alumni Edition)</collection><collection>ProQuest Central UK/Ireland</collection><collection>ProQuest Central Essentials</collection><collection>Biological Science Collection</collection><collection>ProQuest Central</collection><collection>Technology Collection</collection><collection>Natural Science Collection</collection><collection>ProQuest One Community College</collection><collection>ProQuest Materials Science Collection</collection><collection>ProQuest Central Korea</collection><collection>Health Research Premium Collection</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>ProQuest Central Student</collection><collection>SciTech Premium Collection</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>Materials Science Database</collection><collection>ProQuest Biological Science Collection</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>Medical Database</collection><collection>Biological Science Database</collection><collection>Materials Science Collection</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>ProQuest Central China</collection><collection>MEDLINE - Academic</collection><jtitle>Amino acids</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Geng, Pengyu</au><au>Qin, Wangshu</au><au>Xu, Guowang</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Proline metabolism in cancer</atitle><jtitle>Amino acids</jtitle><stitle>Amino Acids</stitle><addtitle>Amino Acids</addtitle><date>2021-12-01</date><risdate>2021</risdate><volume>53</volume><issue>12</issue><spage>1769</spage><epage>1777</epage><pages>1769-1777</pages><issn>0939-4451</issn><eissn>1438-2199</eissn><abstract>Cancer cells often change their metabolism to support uncontrolled proliferation. Proline is the only proteogenic secondary amino acid that is abundant in the body. Recent studies have shown that proline metabolism plays an important role in metabolic reprogramming and affects the occurrence and development of cancer. Proline metabolism is related to ATP production, protein and nucleotide synthesis, and redox homeostasis in tumor cells. Proline can be synthesized by aldehyde dehydrogenase family 18 member A1 (ALDH18A1) and delta1-pyrroline-5-carboxylate reductase (PYCR), up-regulating ALDH18A1 and PYCR can promote the proliferation and invasion of cancer cells. As the main storage of proline, collagen can influence cancer cells proliferation, invasion, and metastasis. Its synthesis depends on the hydroxylation of proline catalyzed by prolyl 4-hydroxylases (P4Hs), which will affect the plasticity and metastasis of cancer cells. The degradation of proline occurs in the mitochondria and involves an oxidation step catalyzed by proline dehydrogenase/proline oxidase (PRODH/POX). Proline catabolism has a dual role in cancer, linking apoptosis with the survival and metastasis of cancer cells. In addition, it has been demonstrated that the regulation of proline metabolic enzymes at the genetic and post-translational levels is related to cancer. This article reviews the role of proline metabolic enzymes in cancer proliferation, apoptosis, metastasis, and development. Research on proline metabolism may provide a new strategy for cancer treatment.</abstract><cop>Vienna</cop><pub>Springer Vienna</pub><pmid>34390414</pmid><doi>10.1007/s00726-021-03060-1</doi><tpages>9</tpages><orcidid>https://orcid.org/0000-0003-4298-3554</orcidid></addata></record> |
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| subjects | Adenosine triphosphate Aldehyde dehydrogenase Aldehydes Amino acids Analytical Chemistry Animals Apoptosis Apoptosis - physiology Biochemical Engineering Biochemistry Biomedical and Life Sciences Cancer Carboxylate reductase Catabolism Cell proliferation Cell Proliferation - physiology Collagen Dehydrogenases Enzymes Homeostasis Humans Hydroxylation Life Sciences Metabolism Metastases Metastasis Mitochondria Neoplasm Metastasis - pathology Neoplasms - metabolism Neoplasms - pathology Neurobiology Nucleotides Oxidation Post-translation Proline Proline - metabolism Proline dehydrogenase Proline metabolism in cancer Proline oxidase Protein biosynthesis Protein turnover Proteomics Pyrroline-5-carboxylate reductase Reductases Review Article Tumor cells |
| title | Proline metabolism in cancer |
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