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J. W. Bauer - One of the best experts on this subject based on the ideXlab platform.

  • sex relAted differences in ChromogrAnin A ChromogrAnin b And secretogrAnin ii gene expression in rAt pituitAry
    Journal of Neuroendocrinology, 1992
    Co-Authors: Reiner Fischercolbrie, K. W. Schmid, Andrea Laslop, Sushil K Mahata, Manjula Mahata, J. W. Bauer
    Abstract:

    ChromogrAnin A, An Acidic secretory protein, is widely distributed throughout diverse endocrine cells And the centrAl And peripherAl nervous systems. ChromogrAnin A is co-stored And co-secreted from secretory vesicles together with the endogenous hormones or neurotrAnsmitters. Recently, two peptides derived from the ChromogrAnin A precursor hAve been shown to inhibit secretion from endocrine cells. In the present study, we investigAted the regulAtion of the biosynthesis of ChromogrAnin A by estrogen in vArious tissues. In the pituitAry, steAdy-stAte levels of ChromogrAnin A mRNA were mArkedly reduced by 64% in estrogen-treAted mAle rAts. At the protein level, A compArAble decreAse wAs found. ChromogrAnin B And secretogrAnin II, two other secretory proteins co-stored with ChromogrAnin A, were slightly increAsed by estrogen. In pituitAries of femAle rAts ChromogrAnin A mRNA And protein levels were significAntly lower thAn in mAles. For ChromogrAnin B on the other hAnd, A 2-fold increAse of mRNA levels wAs found. Our observAtions demonstrAte thAt physiologic concentrAtions of estrogen strongly Affect ChromogrAnin A levels in the pituitAry resulting in A sex-relAted difference in ChromogrAnin A gene expression. BAsed on these And previous results demonstrAting increAsed biosynthesis of ChromogrAnin A by glucocorticoids And cAlciferol, we suggest thAt A typicAl And chArActeristic feAture of the ChromogrAnin A gene is its regulAtion by At leAst three different clAsses of steroid hormones.

  • Sex‐RelAted Differences in ChromogrAnin A, ChromogrAnin B And SecretogrAnin II Gene Expression in RAt PituitAry
    Journal of neuroendocrinology, 1992
    Co-Authors: K. W. Schmid, J. W. Bauer
    Abstract:

    ChromogrAnin A, An Acidic secretory protein, is widely distributed throughout diverse endocrine cells And the centrAl And peripherAl nervous systems. ChromogrAnin A is co-stored And co-secreted from secretory vesicles together with the endogenous hormones or neurotrAnsmitters. Recently, two peptides derived from the ChromogrAnin A precursor hAve been shown to inhibit secretion from endocrine cells. In the present study, we investigAted the regulAtion of the biosynthesis of ChromogrAnin A by estrogen in vArious tissues. In the pituitAry, steAdy-stAte levels of ChromogrAnin A mRNA were mArkedly reduced by 64% in estrogen-treAted mAle rAts. At the protein level, A compArAble decreAse wAs found. ChromogrAnin B And secretogrAnin II, two other secretory proteins co-stored with ChromogrAnin A, were slightly increAsed by estrogen. In pituitAries of femAle rAts ChromogrAnin A mRNA And protein levels were significAntly lower thAn in mAles. For ChromogrAnin B on the other hAnd, A 2-fold increAse of mRNA levels wAs found. Our observAtions demonstrAte thAt physiologic concentrAtions of estrogen strongly Affect ChromogrAnin A levels in the pituitAry resulting in A sex-relAted difference in ChromogrAnin A gene expression. BAsed on these And previous results demonstrAting increAsed biosynthesis of ChromogrAnin A by glucocorticoids And cAlciferol, we suggest thAt A typicAl And chArActeristic feAture of the ChromogrAnin A gene is its regulAtion by At leAst three different clAsses of steroid hormones.

K. W. Schmid - One of the best experts on this subject based on the ideXlab platform.

  • sex relAted differences in ChromogrAnin A ChromogrAnin b And secretogrAnin ii gene expression in rAt pituitAry
    Journal of Neuroendocrinology, 1992
    Co-Authors: Reiner Fischercolbrie, K. W. Schmid, Andrea Laslop, Sushil K Mahata, Manjula Mahata, J. W. Bauer
    Abstract:

    ChromogrAnin A, An Acidic secretory protein, is widely distributed throughout diverse endocrine cells And the centrAl And peripherAl nervous systems. ChromogrAnin A is co-stored And co-secreted from secretory vesicles together with the endogenous hormones or neurotrAnsmitters. Recently, two peptides derived from the ChromogrAnin A precursor hAve been shown to inhibit secretion from endocrine cells. In the present study, we investigAted the regulAtion of the biosynthesis of ChromogrAnin A by estrogen in vArious tissues. In the pituitAry, steAdy-stAte levels of ChromogrAnin A mRNA were mArkedly reduced by 64% in estrogen-treAted mAle rAts. At the protein level, A compArAble decreAse wAs found. ChromogrAnin B And secretogrAnin II, two other secretory proteins co-stored with ChromogrAnin A, were slightly increAsed by estrogen. In pituitAries of femAle rAts ChromogrAnin A mRNA And protein levels were significAntly lower thAn in mAles. For ChromogrAnin B on the other hAnd, A 2-fold increAse of mRNA levels wAs found. Our observAtions demonstrAte thAt physiologic concentrAtions of estrogen strongly Affect ChromogrAnin A levels in the pituitAry resulting in A sex-relAted difference in ChromogrAnin A gene expression. BAsed on these And previous results demonstrAting increAsed biosynthesis of ChromogrAnin A by glucocorticoids And cAlciferol, we suggest thAt A typicAl And chArActeristic feAture of the ChromogrAnin A gene is its regulAtion by At leAst three different clAsses of steroid hormones.

  • Sex‐RelAted Differences in ChromogrAnin A, ChromogrAnin B And SecretogrAnin II Gene Expression in RAt PituitAry
    Journal of neuroendocrinology, 1992
    Co-Authors: K. W. Schmid, J. W. Bauer
    Abstract:

    ChromogrAnin A, An Acidic secretory protein, is widely distributed throughout diverse endocrine cells And the centrAl And peripherAl nervous systems. ChromogrAnin A is co-stored And co-secreted from secretory vesicles together with the endogenous hormones or neurotrAnsmitters. Recently, two peptides derived from the ChromogrAnin A precursor hAve been shown to inhibit secretion from endocrine cells. In the present study, we investigAted the regulAtion of the biosynthesis of ChromogrAnin A by estrogen in vArious tissues. In the pituitAry, steAdy-stAte levels of ChromogrAnin A mRNA were mArkedly reduced by 64% in estrogen-treAted mAle rAts. At the protein level, A compArAble decreAse wAs found. ChromogrAnin B And secretogrAnin II, two other secretory proteins co-stored with ChromogrAnin A, were slightly increAsed by estrogen. In pituitAries of femAle rAts ChromogrAnin A mRNA And protein levels were significAntly lower thAn in mAles. For ChromogrAnin B on the other hAnd, A 2-fold increAse of mRNA levels wAs found. Our observAtions demonstrAte thAt physiologic concentrAtions of estrogen strongly Affect ChromogrAnin A levels in the pituitAry resulting in A sex-relAted difference in ChromogrAnin A gene expression. BAsed on these And previous results demonstrAting increAsed biosynthesis of ChromogrAnin A by glucocorticoids And cAlciferol, we suggest thAt A typicAl And chArActeristic feAture of the ChromogrAnin A gene is its regulAtion by At leAst three different clAsses of steroid hormones.

  • ChromogrAnin A And b in AdenomAs of the pituitAry An immunohistochemicAl study of 42 cAses
    The American Journal of Surgical Pathology, 1991
    Co-Authors: K. W. Schmid, Ruth Hogueangeletti, Martin Tötsch, A. Hittmair, Monika Kroll, Hans Maier, R W Gasser, G Finkenstett, Reiner Fischercolbrie
    Abstract:

    Forty-two pituitAry AdenomAs (10 prolActinomAs; three ACTH-, nine GH-, two FSH- And two TSH-secreting AdenomAs; And 16 clinicAlly nonfunctioning null cell AdenomAs) were investigAted immunohistochemicAlly with Antibodies AgAinst ChromogrAnin A And B As well As ACTH, GH, prolActin (PRL), FSH, LH, TSH, And AlphA-HCG Antibodies. For the demonstrAtion of ChromogrAnin B, two different Antibodies were used--e.g., A polyclonAl AntihumAn Antibody And An Antiserum AgAinst A synthetic peptide (DK-21, ChromogrAnin B 306-326) present in the ChromogrAnin B Amino Acid sequence. All tumors were positive for both ChromogrAnin B Antibodies. ChromogrAnin A wAs found in FSH- (two of two) And TSH- (two of two) secreting AdenomAs; it wAs Also found in A focAl distribution in ACTH- (one of three) And GH- (four of nine) secreting AdenomAs. Thirteen of 16 null cell AdenomAs contAined ChromogrAnin A, whereAs no ChromogrAnin A wAs found in prolActinomAs. We conclude thAt null cell AdenomAs mAy Arise either from FSH/LH or TSH cells (null cell AdenomAs with both ChromogrAnin A And B positivity) or from ACTH, GH, or PRL cells (the respective tumors Are only positive for ChromogrAnin B). ChromogrAnin B mAy be used As A universAl mArker for pituitAry AdenomAs.

  • UndegrAded ChromogrAnin A is present in serum And enters the endocytotic lysosomAl pAthwAy in kidney
    Histochemistry, 1991
    Co-Authors: R. Weiler, K. W. Schmid, H. -j. Steiner, R. Fischer-colbrie, H Winkler
    Abstract:

    AnAlysis of humAn And bovine serum by immunoblotting reveAled the presence of the proprotein ChromogrAnin A. By the sAme method ChromogrAnin A wAs Also found in rAt, bovine And humAn kidney. However this orgAn did not contAin Any ChromogrAnin A mRNA Arguing AgAinst A synthesis within this orgAn. By immun-electron microscopy ChromogrAnin A immunoreActivity wAs found in proximAl tubule cells of rAt kidney. Positive immunostAining wAs present in smAll vesicles within And in close proximity to the brush border And closer to the nucleus in typicAl lysosomAl structures. These results mAke it likely thAt ChromogrAnin A from serum reAches kidney tubule cells by glomerulAr filtrAtion And is tAken up into the endocytotic lysosomAl pAthwAy.

  • ChromogrAnin A And B in pArAthyroid tissue of cAses of primAry hyperpArAthyroidism: An immunohistochemicAl study
    Virchows Archiv A, 1991
    Co-Authors: K. W. Schmid, A. Hittmair, D. Ladurner, P. Sandbichler, R. Gasser, Martin Tötsch
    Abstract:

    Routinely processed pArAthyroid tissues from 26 cAses with primAry hyperpArAthyroidism (19 AdenomAs, 7 multiglAndulAr hyperplAsiA) And 8 normAl humAn pArAthyroid glAnds were investigAted with Antibodies AgAinst ChromogrAnin A And B And pArAthyroid hormone (PTH). NormAl pArAthyroids were immunohistochemicAlly positive for PTH And ChromogrAnin A but negAtive for ChromogrAnin B. HyperplAstic glAnds showed A focAl stAining for PTH And ChromogrAnin A without correlAtion of the stAining pAttern on seriAl sections. AdenomAs were either uniformly positive for both PTH And ChromogrAnin A or showed A stAining pAttern similAr to thAt seen in hyperplAstic glAnds. FocAl ChromogrAnin B positivity (less thAn 10% of cells) wAs found in 3 cAses (1 hyperplAstic glAnd And 2 cAses of pArAthyroid AdenomA with An immunohistochemicAl stAining pAttern similAr to hyperplAstic glAnds). Our immunohistochemicAl results mAy support previously published findings thAt most pArAthyroid AdenomAs Are monoclonAl neoplAsms whereAs hyperplAstic glAnds Are of polyclonAl origin.

Daniel T. O'connor - One of the best experts on this subject based on the ideXlab platform.

  • Glucocorticoid ActivAtion of ChromogrAnin A gene expression. IdentificAtion And chArActerizAtion of A novel glucocorticoid response element.
    The Journal of clinical investigation, 1994
    Co-Authors: David J. Rozansky, Robert J. Parmer, Kechun Tang, Daniel T. O'connor
    Abstract:

    Glucocorticoids regulAte cAtecholAmine biosynthesis And storAge At severAl sites. ChromogrAnin A, An AbundAnt protein complexed with cAtecholAmines in secretory vesicles of chromAffin cells And sympAthetic Axons, is Also Augmented by glucocorticoids. This study reports isolAtion of the rAt ChromogrAnin A promoter to elucidAte trAnscriptionAl regulAtion of ChromogrAnin A biosynthesis by glucocorticoids in neuroendocrine cells. Endogenous ChromogrAnin A gene expression wAs ActivAted up to 3.5-fold in chromAffin cells by glucocorticoid, in time-dependent fAshion. Inhibition of new protein synthesis by cycloheximide did not Alter the rise in ChromogrAnin A mRNA, suggesting thAt glucocorticoids directly ActivAte the ChromogrAnin A promoter; nucleAr runoff AssAys confirmed A 3.3-fold increAsed rAte of initiAtion of new ChromogrAnin A trAnscripts After glucocorticoid. TrAnsfected rAt ChromogrAnin A promoter/luciferAse reporter constructs were ActivAted 2.6-3.1-fold by glucocorticoid, And selective Agonist/AntAgonist studies determined thAt dexAmethAsone effects were mediAted by glucocorticoid receptors. Both rAt And mouse ChromogrAnin A promoter/luciferAse reporter constructs were ActivAted by glucocorticoid. A series of promoter deletions nArrowed the region of glucocorticoid Action to A 93-bp section of the promoter, from position -526 to -619 bp upstreAm of the cAp site. A 15-bp sequence ([-583 bp] 5'-ACATGAGTGTGTCCT-3' [-597 bp]) within this region showed pArtiAl homology to A glucocorticoid response element (GRE; hAlf-site in itAlics) consensus sequence, And severAl lines of experimentAl evidence confirmed its function As A GRE: (A) site-directed mutAtion of this GRE prevented glucocorticoid ActivAtion of A ChromogrAnin A promoter/reporter; (b) trAnsfer of this GRE to A heterologous (thymidine kinAse) promoter/reporter conferred ActivAtion by glucocorticoid, in copy number-dependent And orientAtion-independent fAshion; And (c) electrophoretic gel mobility shifts demonstrAted binding of this GRE by ligAnd-ActivAted glucocorticoid receptor, though At 2.75-fold lower Affinity thAn the glucocorticoid receptor interAction with A consensus GRE. The rAt ChromogrAnin A GRE showed functionAl And structurAl similArities to GREs in other genes proportionAlly regulAted by glucocorticoids. We conclude thAt A discrete domAin of the ChromogrAnin A promoter is both necessAry And sufficient to confer glucocorticoid regulAtion onto the gene, And thAt the Activity of this region Also explAins the degree of ActivAtion of the endogenous gene by glucocorticoid.

  • Assignment of the ChromogrAnin A (chgA) locus to homologous regions on mouse chromosome 12 And rAt chromosome 6
    Genomics, 1993
    Co-Authors: Dominique Simon-chazottes, David J. Rozansky, Hongjiang Wu, Robert J. Parmer, Josiane Szpirer, Theodore W. Kurtz, Claude Szpirer, Jean-louis Guénet, Göran Levan, Daniel T. O'connor
    Abstract:

    ChromogrAnin A is An Acidic protein, stored And releAsed with cAtecholAmines, And is overexpressed in genetic hypertension. In the humAn genome, its locus hAs previously been positioned on the long Arm of Chromosome 14 in the 14q32 region. As A first step towArd evAluAting its potentiAl linkAge with hereditAry hypertension, we determined its chromosomAl position in mouse And rAt. ChromogrAnin A wAs present As A single-copy gene in both mouse And rAt. AnAlysis of the Allele distribution in An interspecific mouse bAckcross by single-strAnd conformAtion polymorphism positioned the ChromogrAnin A locus on Chromosome 12, between Igh-C And D12PAs1. EvAluAtion of A rAt/mouse somAtic cell hybrid pAnel indicAted thAt ChromogrAnin A is on rAt Chromosome 6. In eAch cAse (mouse, rAt, And humAn), ChromogrAnin A is in A conserved region with neArby mArkers including the immunoglobulin heAvy chAin locus.

  • ChromogrAnin A: PosttrAnslAtionAl ModificAtions in Secretory GrAnules
    Endocrinology, 1991
    Co-Authors: Juan A. Barbosa, Bruce M. Gill, Marwan A. Takiyyuddin, Daniel T. O'connor
    Abstract:

    The primAry structure of ChromogrAnin A indicAtes multiple domAins which might be subject to posttrAnslAtionAl modificAtion. We explored ChromogrAnin A’s proteolytic cleAvAge, glycosylAtion, And possible intermoleculAr disulfide links, using biochemicAl And cell biologicAl ApproAches. AntiChromogrAnin A region-specific immunoblots on chromAffin grAnules suggested bidirectionAl endoproteolytic cleAvAge of ChromogrAnin A; control experiments ruled out ArtifActuAl cleAvAge during grAnule isolAtion or lysis. IsolAtion of ChromogrAnin A-derived peptides by gel filtrAtion chromAtogrAphy or sodium dodecyl sulfAte-polyAcrylAmide gel electrophoresis (SDSPAGE), followed by N-terminAl Amino Acid sequencing, estAblished severAl cleAvAge sites, including At leAst two At dibAsic sites. Secretion of ChromogrAnin A from bovine chromAffin cells did not initiAte further cleAvAge, nor did prolonged exposure of secreted ChromogrAnins to the secretory cells. The ChromogrAnin A cleAvAge pAttern wAs quAlitAtively similAr in oth...

  • ChromogrAnin A storAge And secretion: sensitivity And specificity for the diAgnosis of pheochromocytomA.
    Medicine, 1991
    Co-Authors: Ray J. Hsiao, Marwan A. Takiyyuddin, Robert J. Parmer, Daniel T. O'connor
    Abstract:

    ChromogrAnin A, co-stored And co-releAsed with cAtecholAmines from AdrenAl medullAry And sympAthetic neuronAl vesicles, is elevAted in the plAsmA of pAtients with pheochromocytomA. The usefulness of the hormone in the differentiAl diAgnosis of hypertension is exAmined. An elevAted level of ChromogrAnin A hAd compArAble diAgnostic sensitivity (83%, 24/29) to, but greAter diAgnostic specificity (96%, 86/90) thAn the level of plAsmA cAtecholAmines when subjects with pheochromocytomA (n = 29) were evAluAted in compArison to severAl reference groups, including normotensive controls (n = 49), subjects with essentiAl hypertension (n = 28), subjects with renovAsculAr hypertension (n = 5), And subjects with primAry Aldosteronism (n = 3). Subjects with signs or symptoms suggesting pheochromocytomA, but in whom the diAgnosis wAs ultimAtely ruled out (n = 5) hAd normAl plAsmA levels of ChromogrAnin A. A modest rise in ChromogrAnin A in those with essentiAl hypertension, And correlAtion of ChromogrAnin A with diAstolic blood pressure in normotensive pAtients And pAtients with essentiAl hypertension did not impAir the diAgnostic usefulness of ChromogrAnin A for pheochromocytomA. RenAl fAilure wAs AssociAted with An elevAted plAsmA ChromogrAnin A independently of blood pressure. PlAsmA ChromogrAnin A correlAted with tumor mAss, tumor ChromogrAnin A content, tumor norepinephrine content, And urinAry vAnillylmAndelic Acid excretion; it did not correlAte with plAsmA or urinAry cAtecholAmines, nor with blood pressure in pAtients with pheochromocytomA. PlAsmA ChromogrAnin A levels did not differ in subjects with pheochromocytomA when strAtified by Age, sex, tumor locAtion, or tumor pAthology. SeverAl drugs used in the diAgnosis or treAtment of pheochromocytomA (clonidine, metoprolol, phentolAmine, And tyrAmine) hAd little effect on plAsmA ChromogrAnin A concentrAtion. Within the pheochromocytomA, ChromogrAnin A wAs locAlized Along with cAtecholAmines to the soluble core of chromAffin grAnules, where it Accounted for 18 +/- 5% of vesicle soluble protein. We conclude thAt 1) ChromogrAnin A emerges Along with cAtecholAmines from pheochromocytomA chromAffin grAnules; 2) plAsmA ChromogrAnin A is A sensitive And specific diAgnostic tool in evAluAtion of ActuAl or suspected pheochromocytomA; 3) plAsmA ChromogrAnin A predicts pheochromocytomA tumor size And overAll cAtecholAmine production; And 4) drugs commonly employed in the diAgnosis or treAtment of pheochromocytomA hAve little effect on plAsmA ChromogrAnin A level, preserving the usefulness of ChromogrAnin A in evAluAting pheochromocytomA. Thus, meAsurement of ChromogrAnin A provides A useful Adjunct to the diAgnosis of pheochromocytomA.

Irvin M. Modlin - One of the best experts on this subject based on the ideXlab platform.

  • ChromogrAnin A Any relevAnce in neuroendocrine tumors
    Current Opinion in Endocrinology Diabetes and Obesity, 2016
    Co-Authors: Mark Kidd, Lisa Bodei, Irvin M. Modlin
    Abstract:

    Purpose of reviewThe review summArizes the utility And limitAtions of ChromogrAnin A (CgA) As A circulAting biomArker for neuroendocrine tumors (NETs).Recent findingsBlood CgA meAsurement hAs numerous clinicAl limitAtions including poor AssAy reproducibility, low sensitivity (metA-AnAlysis: 73%, 95%

  • The ClinicAl RelevAnce of ChromogrAnin A As A BiomArker for GAstroenteropAncreAtic Neuroendocrine Tumors
    Endocrinology and metabolism clinics of North America, 2011
    Co-Authors: Ben Lawrence, Bjorn I. Gustafsson, Mark Kidd, Marianne Pavel, Bernhard Svejda, Irvin M. Modlin
    Abstract:

    ChromogrAnin A, Although it exhibits limitAtions, is currently the most useful generAl tumor biomArker AvAilAble for use in the diAgnosis And mAnAgement of gAstroenteropAncreAtic neuroendocrine tumors (NETs). The vAlue of the ChromogrAnin A lies in its universAl cosecretion by the mAjority of neuroendocrine cells thAt persists After mAlignAnt trAnsformAtion. CliniciAns AwAre of the physiologic role of ChromogrAnin A And its secretion in A vAriety of non-NET-relAted pAthologic conditions cAn use this protein As A moderAtely effective tumor biomArker in the mAnAgement of GEP-NETs.

Reiner Fischercolbrie - One of the best experts on this subject based on the ideXlab platform.

  • sex relAted differences in ChromogrAnin A ChromogrAnin b And secretogrAnin ii gene expression in rAt pituitAry
    Journal of Neuroendocrinology, 1992
    Co-Authors: Reiner Fischercolbrie, K. W. Schmid, Andrea Laslop, Sushil K Mahata, Manjula Mahata, J. W. Bauer
    Abstract:

    ChromogrAnin A, An Acidic secretory protein, is widely distributed throughout diverse endocrine cells And the centrAl And peripherAl nervous systems. ChromogrAnin A is co-stored And co-secreted from secretory vesicles together with the endogenous hormones or neurotrAnsmitters. Recently, two peptides derived from the ChromogrAnin A precursor hAve been shown to inhibit secretion from endocrine cells. In the present study, we investigAted the regulAtion of the biosynthesis of ChromogrAnin A by estrogen in vArious tissues. In the pituitAry, steAdy-stAte levels of ChromogrAnin A mRNA were mArkedly reduced by 64% in estrogen-treAted mAle rAts. At the protein level, A compArAble decreAse wAs found. ChromogrAnin B And secretogrAnin II, two other secretory proteins co-stored with ChromogrAnin A, were slightly increAsed by estrogen. In pituitAries of femAle rAts ChromogrAnin A mRNA And protein levels were significAntly lower thAn in mAles. For ChromogrAnin B on the other hAnd, A 2-fold increAse of mRNA levels wAs found. Our observAtions demonstrAte thAt physiologic concentrAtions of estrogen strongly Affect ChromogrAnin A levels in the pituitAry resulting in A sex-relAted difference in ChromogrAnin A gene expression. BAsed on these And previous results demonstrAting increAsed biosynthesis of ChromogrAnin A by glucocorticoids And cAlciferol, we suggest thAt A typicAl And chArActeristic feAture of the ChromogrAnin A gene is its regulAtion by At leAst three different clAsses of steroid hormones.

  • ChromogrAnin A And b in AdenomAs of the pituitAry An immunohistochemicAl study of 42 cAses
    The American Journal of Surgical Pathology, 1991
    Co-Authors: K. W. Schmid, Ruth Hogueangeletti, Martin Tötsch, A. Hittmair, Monika Kroll, Hans Maier, R W Gasser, G Finkenstett, Reiner Fischercolbrie
    Abstract:

    Forty-two pituitAry AdenomAs (10 prolActinomAs; three ACTH-, nine GH-, two FSH- And two TSH-secreting AdenomAs; And 16 clinicAlly nonfunctioning null cell AdenomAs) were investigAted immunohistochemicAlly with Antibodies AgAinst ChromogrAnin A And B As well As ACTH, GH, prolActin (PRL), FSH, LH, TSH, And AlphA-HCG Antibodies. For the demonstrAtion of ChromogrAnin B, two different Antibodies were used--e.g., A polyclonAl AntihumAn Antibody And An Antiserum AgAinst A synthetic peptide (DK-21, ChromogrAnin B 306-326) present in the ChromogrAnin B Amino Acid sequence. All tumors were positive for both ChromogrAnin B Antibodies. ChromogrAnin A wAs found in FSH- (two of two) And TSH- (two of two) secreting AdenomAs; it wAs Also found in A focAl distribution in ACTH- (one of three) And GH- (four of nine) secreting AdenomAs. Thirteen of 16 null cell AdenomAs contAined ChromogrAnin A, whereAs no ChromogrAnin A wAs found in prolActinomAs. We conclude thAt null cell AdenomAs mAy Arise either from FSH/LH or TSH cells (null cell AdenomAs with both ChromogrAnin A And B positivity) or from ACTH, GH, or PRL cells (the respective tumors Are only positive for ChromogrAnin B). ChromogrAnin B mAy be used As A universAl mArker for pituitAry AdenomAs.