Chemistry and biosynthesis of pro-opiomelanocortin
Summary Studies of lipotropins, melanotropins and endorphins on one hand, and of adrenocorticotropin on the other, has given rise to the concept of a multipotent precursor molecule recently renamed proopiomelanocortin. The preferential sites of cleavage of the precursor to produce its biologically a...
Ausführliche Beschreibung
Gespeichert in:
| Autor*in: |
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| Format: |
E-Artikel |
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| Sprache: |
Englisch |
| Erschienen: |
1981 |
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| Umfang: |
27 |
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| Reproduktion: |
Springer Online Journal Archives 1860-2002 |
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| Übergeordnetes Werk: |
in: Molecular and cellular biochemistry - 1973, 34(1981) vom: Feb., Seite 101-127 |
| Übergeordnetes Werk: |
volume:34 ; year:1981 ; month:02 ; pages:101-127 ; extent:27 |
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| 520 | |a Summary Studies of lipotropins, melanotropins and endorphins on one hand, and of adrenocorticotropin on the other, has given rise to the concept of a multipotent precursor molecule recently renamed proopiomelanocortin. The preferential sites of cleavage of the precursor to produce its biologically active components are made of pairs of basic amino acid residues as described for the biosynthesis of beta-MSH and pro-insulin. Such structure is also found in other pro-hormone molecules. Pulse chase experiments and secretory studies carried out in both anterior and intermediate lobes of rat pituitary glands revealed the transformation of different forms of the precursor into different end-products, the anterior lobe producing preferentially ACTH and beta-LPH while the intermediate produces mainly alpha-MSH and beta-endorphin. The multiple forms of precursors seem to differ in their carbohydrate content althouth at least two different gene products are still possible. The presence of similar peptides in the hypothalamus makes it highly probable that neuropeptides are biosynthesized with similar process. Thus the model of beta-LPH precursor, proposed as early as in 1967, is now applicable to the biosynthesis of all other neuropeptides. Major advances in this field are expected in the 1980's. | ||
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(DE-627)NLEJ198058179 DE-627 ger DE-627 rakwb eng Chemistry and biosynthesis of pro-opiomelanocortin 1981 27 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Summary Studies of lipotropins, melanotropins and endorphins on one hand, and of adrenocorticotropin on the other, has given rise to the concept of a multipotent precursor molecule recently renamed proopiomelanocortin. The preferential sites of cleavage of the precursor to produce its biologically active components are made of pairs of basic amino acid residues as described for the biosynthesis of beta-MSH and pro-insulin. Such structure is also found in other pro-hormone molecules. Pulse chase experiments and secretory studies carried out in both anterior and intermediate lobes of rat pituitary glands revealed the transformation of different forms of the precursor into different end-products, the anterior lobe producing preferentially ACTH and beta-LPH while the intermediate produces mainly alpha-MSH and beta-endorphin. The multiple forms of precursors seem to differ in their carbohydrate content althouth at least two different gene products are still possible. The presence of similar peptides in the hypothalamus makes it highly probable that neuropeptides are biosynthesized with similar process. Thus the model of beta-LPH precursor, proposed as early as in 1967, is now applicable to the biosynthesis of all other neuropeptides. Major advances in this field are expected in the 1980's. Springer Online Journal Archives 1860-2002 Chrétien, Michel oth Seidah, N. G. oth in Molecular and cellular biochemistry 1973 34(1981) vom: Feb., Seite 101-127 (DE-627)NLEJ188989099 (DE-600)2003615-2 1573-4919 nnns volume:34 year:1981 month:02 pages:101-127 extent:27 http://dx.doi.org/10.1007/BF02354864 GBV_USEFLAG_U ZDB-1-SOJ GBV_NL_ARTICLE AR 34 1981 2 101-127 27 |
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(DE-627)NLEJ198058179 DE-627 ger DE-627 rakwb eng Chemistry and biosynthesis of pro-opiomelanocortin 1981 27 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Summary Studies of lipotropins, melanotropins and endorphins on one hand, and of adrenocorticotropin on the other, has given rise to the concept of a multipotent precursor molecule recently renamed proopiomelanocortin. The preferential sites of cleavage of the precursor to produce its biologically active components are made of pairs of basic amino acid residues as described for the biosynthesis of beta-MSH and pro-insulin. Such structure is also found in other pro-hormone molecules. Pulse chase experiments and secretory studies carried out in both anterior and intermediate lobes of rat pituitary glands revealed the transformation of different forms of the precursor into different end-products, the anterior lobe producing preferentially ACTH and beta-LPH while the intermediate produces mainly alpha-MSH and beta-endorphin. The multiple forms of precursors seem to differ in their carbohydrate content althouth at least two different gene products are still possible. The presence of similar peptides in the hypothalamus makes it highly probable that neuropeptides are biosynthesized with similar process. Thus the model of beta-LPH precursor, proposed as early as in 1967, is now applicable to the biosynthesis of all other neuropeptides. Major advances in this field are expected in the 1980's. Springer Online Journal Archives 1860-2002 Chrétien, Michel oth Seidah, N. G. oth in Molecular and cellular biochemistry 1973 34(1981) vom: Feb., Seite 101-127 (DE-627)NLEJ188989099 (DE-600)2003615-2 1573-4919 nnns volume:34 year:1981 month:02 pages:101-127 extent:27 http://dx.doi.org/10.1007/BF02354864 GBV_USEFLAG_U ZDB-1-SOJ GBV_NL_ARTICLE AR 34 1981 2 101-127 27 |
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(DE-627)NLEJ198058179 DE-627 ger DE-627 rakwb eng Chemistry and biosynthesis of pro-opiomelanocortin 1981 27 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Summary Studies of lipotropins, melanotropins and endorphins on one hand, and of adrenocorticotropin on the other, has given rise to the concept of a multipotent precursor molecule recently renamed proopiomelanocortin. The preferential sites of cleavage of the precursor to produce its biologically active components are made of pairs of basic amino acid residues as described for the biosynthesis of beta-MSH and pro-insulin. Such structure is also found in other pro-hormone molecules. Pulse chase experiments and secretory studies carried out in both anterior and intermediate lobes of rat pituitary glands revealed the transformation of different forms of the precursor into different end-products, the anterior lobe producing preferentially ACTH and beta-LPH while the intermediate produces mainly alpha-MSH and beta-endorphin. The multiple forms of precursors seem to differ in their carbohydrate content althouth at least two different gene products are still possible. The presence of similar peptides in the hypothalamus makes it highly probable that neuropeptides are biosynthesized with similar process. Thus the model of beta-LPH precursor, proposed as early as in 1967, is now applicable to the biosynthesis of all other neuropeptides. Major advances in this field are expected in the 1980's. Springer Online Journal Archives 1860-2002 Chrétien, Michel oth Seidah, N. G. oth in Molecular and cellular biochemistry 1973 34(1981) vom: Feb., Seite 101-127 (DE-627)NLEJ188989099 (DE-600)2003615-2 1573-4919 nnns volume:34 year:1981 month:02 pages:101-127 extent:27 http://dx.doi.org/10.1007/BF02354864 GBV_USEFLAG_U ZDB-1-SOJ GBV_NL_ARTICLE AR 34 1981 2 101-127 27 |
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(DE-627)NLEJ198058179 DE-627 ger DE-627 rakwb eng Chemistry and biosynthesis of pro-opiomelanocortin 1981 27 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Summary Studies of lipotropins, melanotropins and endorphins on one hand, and of adrenocorticotropin on the other, has given rise to the concept of a multipotent precursor molecule recently renamed proopiomelanocortin. The preferential sites of cleavage of the precursor to produce its biologically active components are made of pairs of basic amino acid residues as described for the biosynthesis of beta-MSH and pro-insulin. Such structure is also found in other pro-hormone molecules. Pulse chase experiments and secretory studies carried out in both anterior and intermediate lobes of rat pituitary glands revealed the transformation of different forms of the precursor into different end-products, the anterior lobe producing preferentially ACTH and beta-LPH while the intermediate produces mainly alpha-MSH and beta-endorphin. The multiple forms of precursors seem to differ in their carbohydrate content althouth at least two different gene products are still possible. The presence of similar peptides in the hypothalamus makes it highly probable that neuropeptides are biosynthesized with similar process. Thus the model of beta-LPH precursor, proposed as early as in 1967, is now applicable to the biosynthesis of all other neuropeptides. Major advances in this field are expected in the 1980's. Springer Online Journal Archives 1860-2002 Chrétien, Michel oth Seidah, N. G. oth in Molecular and cellular biochemistry 1973 34(1981) vom: Feb., Seite 101-127 (DE-627)NLEJ188989099 (DE-600)2003615-2 1573-4919 nnns volume:34 year:1981 month:02 pages:101-127 extent:27 http://dx.doi.org/10.1007/BF02354864 GBV_USEFLAG_U ZDB-1-SOJ GBV_NL_ARTICLE AR 34 1981 2 101-127 27 |
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(DE-627)NLEJ198058179 DE-627 ger DE-627 rakwb eng Chemistry and biosynthesis of pro-opiomelanocortin 1981 27 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Summary Studies of lipotropins, melanotropins and endorphins on one hand, and of adrenocorticotropin on the other, has given rise to the concept of a multipotent precursor molecule recently renamed proopiomelanocortin. The preferential sites of cleavage of the precursor to produce its biologically active components are made of pairs of basic amino acid residues as described for the biosynthesis of beta-MSH and pro-insulin. Such structure is also found in other pro-hormone molecules. Pulse chase experiments and secretory studies carried out in both anterior and intermediate lobes of rat pituitary glands revealed the transformation of different forms of the precursor into different end-products, the anterior lobe producing preferentially ACTH and beta-LPH while the intermediate produces mainly alpha-MSH and beta-endorphin. The multiple forms of precursors seem to differ in their carbohydrate content althouth at least two different gene products are still possible. The presence of similar peptides in the hypothalamus makes it highly probable that neuropeptides are biosynthesized with similar process. Thus the model of beta-LPH precursor, proposed as early as in 1967, is now applicable to the biosynthesis of all other neuropeptides. Major advances in this field are expected in the 1980's. Springer Online Journal Archives 1860-2002 Chrétien, Michel oth Seidah, N. G. oth in Molecular and cellular biochemistry 1973 34(1981) vom: Feb., Seite 101-127 (DE-627)NLEJ188989099 (DE-600)2003615-2 1573-4919 nnns volume:34 year:1981 month:02 pages:101-127 extent:27 http://dx.doi.org/10.1007/BF02354864 GBV_USEFLAG_U ZDB-1-SOJ GBV_NL_ARTICLE AR 34 1981 2 101-127 27 |
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Summary Studies of lipotropins, melanotropins and endorphins on one hand, and of adrenocorticotropin on the other, has given rise to the concept of a multipotent precursor molecule recently renamed proopiomelanocortin. The preferential sites of cleavage of the precursor to produce its biologically active components are made of pairs of basic amino acid residues as described for the biosynthesis of beta-MSH and pro-insulin. Such structure is also found in other pro-hormone molecules. Pulse chase experiments and secretory studies carried out in both anterior and intermediate lobes of rat pituitary glands revealed the transformation of different forms of the precursor into different end-products, the anterior lobe producing preferentially ACTH and beta-LPH while the intermediate produces mainly alpha-MSH and beta-endorphin. The multiple forms of precursors seem to differ in their carbohydrate content althouth at least two different gene products are still possible. The presence of similar peptides in the hypothalamus makes it highly probable that neuropeptides are biosynthesized with similar process. Thus the model of beta-LPH precursor, proposed as early as in 1967, is now applicable to the biosynthesis of all other neuropeptides. Major advances in this field are expected in the 1980's. |
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Summary Studies of lipotropins, melanotropins and endorphins on one hand, and of adrenocorticotropin on the other, has given rise to the concept of a multipotent precursor molecule recently renamed proopiomelanocortin. The preferential sites of cleavage of the precursor to produce its biologically active components are made of pairs of basic amino acid residues as described for the biosynthesis of beta-MSH and pro-insulin. Such structure is also found in other pro-hormone molecules. Pulse chase experiments and secretory studies carried out in both anterior and intermediate lobes of rat pituitary glands revealed the transformation of different forms of the precursor into different end-products, the anterior lobe producing preferentially ACTH and beta-LPH while the intermediate produces mainly alpha-MSH and beta-endorphin. The multiple forms of precursors seem to differ in their carbohydrate content althouth at least two different gene products are still possible. The presence of similar peptides in the hypothalamus makes it highly probable that neuropeptides are biosynthesized with similar process. Thus the model of beta-LPH precursor, proposed as early as in 1967, is now applicable to the biosynthesis of all other neuropeptides. Major advances in this field are expected in the 1980's. |
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Summary Studies of lipotropins, melanotropins and endorphins on one hand, and of adrenocorticotropin on the other, has given rise to the concept of a multipotent precursor molecule recently renamed proopiomelanocortin. The preferential sites of cleavage of the precursor to produce its biologically active components are made of pairs of basic amino acid residues as described for the biosynthesis of beta-MSH and pro-insulin. Such structure is also found in other pro-hormone molecules. Pulse chase experiments and secretory studies carried out in both anterior and intermediate lobes of rat pituitary glands revealed the transformation of different forms of the precursor into different end-products, the anterior lobe producing preferentially ACTH and beta-LPH while the intermediate produces mainly alpha-MSH and beta-endorphin. The multiple forms of precursors seem to differ in their carbohydrate content althouth at least two different gene products are still possible. The presence of similar peptides in the hypothalamus makes it highly probable that neuropeptides are biosynthesized with similar process. Thus the model of beta-LPH precursor, proposed as early as in 1967, is now applicable to the biosynthesis of all other neuropeptides. Major advances in this field are expected in the 1980's. |
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<?xml version="1.0" encoding="UTF-8"?><collection xmlns="http://www.loc.gov/MARC21/slim"><record><leader>01000caa a22002652 4500</leader><controlfield tag="001">NLEJ198058179</controlfield><controlfield tag="003">DE-627</controlfield><controlfield tag="005">20210705232149.0</controlfield><controlfield tag="007">cr uuu---uuuuu</controlfield><controlfield tag="008">070527s1981 xx |||||o 00| ||eng c</controlfield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(DE-627)NLEJ198058179</subfield></datafield><datafield tag="040" ind1=" " ind2=" "><subfield code="a">DE-627</subfield><subfield code="b">ger</subfield><subfield code="c">DE-627</subfield><subfield code="e">rakwb</subfield></datafield><datafield tag="041" ind1=" " ind2=" "><subfield code="a">eng</subfield></datafield><datafield tag="245" ind1="1" ind2="0"><subfield code="a">Chemistry and biosynthesis of pro-opiomelanocortin</subfield></datafield><datafield tag="264" ind1=" " ind2="1"><subfield code="c">1981</subfield></datafield><datafield tag="300" ind1=" " ind2=" "><subfield code="a">27</subfield></datafield><datafield tag="336" ind1=" " ind2=" "><subfield code="a">nicht spezifiziert</subfield><subfield code="b">zzz</subfield><subfield code="2">rdacontent</subfield></datafield><datafield tag="337" ind1=" " ind2=" "><subfield code="a">nicht spezifiziert</subfield><subfield code="b">z</subfield><subfield code="2">rdamedia</subfield></datafield><datafield tag="338" ind1=" " ind2=" "><subfield code="a">nicht spezifiziert</subfield><subfield code="b">zu</subfield><subfield code="2">rdacarrier</subfield></datafield><datafield tag="520" ind1=" " ind2=" "><subfield code="a">Summary Studies of lipotropins, melanotropins and endorphins on one hand, and of adrenocorticotropin on the other, has given rise to the concept of a multipotent precursor molecule recently renamed proopiomelanocortin. The preferential sites of cleavage of the precursor to produce its biologically active components are made of pairs of basic amino acid residues as described for the biosynthesis of beta-MSH and pro-insulin. Such structure is also found in other pro-hormone molecules. Pulse chase experiments and secretory studies carried out in both anterior and intermediate lobes of rat pituitary glands revealed the transformation of different forms of the precursor into different end-products, the anterior lobe producing preferentially ACTH and beta-LPH while the intermediate produces mainly alpha-MSH and beta-endorphin. The multiple forms of precursors seem to differ in their carbohydrate content althouth at least two different gene products are still possible. The presence of similar peptides in the hypothalamus makes it highly probable that neuropeptides are biosynthesized with similar process. Thus the model of beta-LPH precursor, proposed as early as in 1967, is now applicable to the biosynthesis of all other neuropeptides. Major advances in this field are expected in the 1980's.</subfield></datafield><datafield tag="533" ind1=" " ind2=" "><subfield code="f">Springer Online Journal Archives 1860-2002</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Chrétien, Michel</subfield><subfield code="4">oth</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Seidah, N. G.</subfield><subfield code="4">oth</subfield></datafield><datafield tag="773" ind1="0" ind2="8"><subfield code="i">in</subfield><subfield code="t">Molecular and cellular biochemistry</subfield><subfield code="d">1973</subfield><subfield code="g">34(1981) vom: Feb., Seite 101-127</subfield><subfield code="w">(DE-627)NLEJ188989099</subfield><subfield code="w">(DE-600)2003615-2</subfield><subfield code="x">1573-4919</subfield><subfield code="7">nnns</subfield></datafield><datafield tag="773" ind1="1" ind2="8"><subfield code="g">volume:34</subfield><subfield code="g">year:1981</subfield><subfield code="g">month:02</subfield><subfield code="g">pages:101-127</subfield><subfield code="g">extent:27</subfield></datafield><datafield tag="856" ind1="4" ind2="0"><subfield code="u">http://dx.doi.org/10.1007/BF02354864</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_USEFLAG_U</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">ZDB-1-SOJ</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_NL_ARTICLE</subfield></datafield><datafield tag="951" ind1=" " ind2=" "><subfield code="a">AR</subfield></datafield><datafield tag="952" ind1=" " ind2=" "><subfield code="d">34</subfield><subfield code="j">1981</subfield><subfield code="c">2</subfield><subfield code="h">101-127</subfield><subfield code="g">27</subfield></datafield></record></collection>
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