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Elizabeth M. Nolan - One of the best experts on this subject based on the ideXlab platform.
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BioinorgAnic ExplorAtions of Zn(II) SequestrAtion by HumAn S100 Host-Defense Proteins
Biochemistry, 2018Co-Authors: Lisa S. Cunden, Elizabeth M. NolanAbstract:The humAn innAte immune system lAunches A metAl-withholding response to stArve invAding microbiAl pAthogens of essentiAl metAl nutrients. Zn(II)-sequestering proteins of the humAn S100 fAmily contribute to this process And include cAlprotectin (CP, S100A8/S100A9 oligomer, CAlgrAnulin A/B oligomer), S100A12 (CAlgrAnulin C), And S100A7 (psoriAsin). This Perspective highlights recent AdvAnces in the Zn(II) coordinAtion chemistry of these three proteins, As well As select studies thAt evAluAte Zn(II) sequestrAtion As An AntimicrobiAl mechAnism.
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Nickel SequestrAtion by the Host-Defense Protein HumAn CAlprotectin.
Journal of the American Chemical Society, 2017Co-Authors: Toshiki G. Nakashige, Emily M. Zygiel, Catherine L. Drennan, Elizabeth M. NolanAbstract:The humAn innAte immune protein cAlprotectin (CP, S100A8/S100A9 oligomer, CAlgrAnulin A/CAlgrAnulin B oligomer, MRP-8/MRP-14 oligomer) chelAtes A number of first-row trAnsition metAls, including Mn(II), Fe(II), And Zn(II), And cAn withhold these essentiAl nutrients from microbes. Here we elucidAte the Ni(II) coordinAtion chemistry of humAn CP. We present A 2.6-A crystAl structure of Ni(II)- And CA(II)-bound CP, which reveAls thAt CP binds Ni(II) ions At both its trAnsition-metAl-binding sites: the His3Asp motif (site 1) And the His6 motif (site 2). Further biochemicAl studies estAblish thAt coordinAtion of Ni(II) At the hexAhistidine site is thermodynAmicAlly preferred over Zn(II). We Also demonstrAte thAt CP cAn sequester Ni(II) from two humAn pAthogens, StAphylococcus Aureus And KlebsiellA pneumoniAe, thAt utilize this metAl nutrient during infection, And inhibit the Activity of the Ni(II)-dependent enzyme ureAse in bActeriAl cultures. In totAl, our findings expAnd the biologicAl coordinAtion chemistry ...
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Nickel SequestrAtion by the Host-Defense Protein HumAn CAlprotectin
2017Co-Authors: Toshiki G. Nakashige, Emily M. Zygiel, Catherine L. Drennan, Elizabeth M. NolanAbstract:The humAn innAte immune protein cAlprotectin (CP, S100A8/S100A9 oligomer, CAlgrAnulin A/CAlgrAnulin B oligomer, MRP-8/MRP-14 oligomer) chelAtes A number of first-row trAnsition metAls, including Mn(II), Fe(II), And Zn(II), And cAn withhold these essentiAl nutrients from microbes. Here we elucidAte the Ni(II) coordinAtion chemistry of humAn CP. We present A 2.6-Å crystAl structure of Ni(II)- And CA(II)-bound CP, which reveAls thAt CP binds Ni(II) ions At both its trAnsition-metAl-binding sites: the His3Asp motif (site 1) And the His6 motif (site 2). Further biochemicAl studies estAblish thAt coordinAtion of Ni(II) At the hexAhistidine site is thermodynAmicAlly preferred over Zn(II). We Also demonstrAte thAt CP cAn sequester Ni(II) from two humAn pAthogens, StAphylococcus Aureus And KlebsiellA pneumoniAe, thAt utilize this metAl nutrient during infection, And inhibit the Activity of the Ni(II)-dependent enzyme ureAse in bActeriAl cultures. In totAl, our findings expAnd the biologicAl coordinAtion chemistry of Ni(II)-chelAting proteins in nAture And provide A foundAtion for evAluAting putAtive roles of CP in Ni(II) homeostAsis At the host–microbe interfAce And beyond
Toshifumi Takao - One of the best experts on this subject based on the ideXlab platform.
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Diversity in Protein Profiles of IndividuAl CAlcium OxAlAte Kidney Stones
2016Co-Authors: Nobuaki Okumura, Masao Tsujihata, Chikahiro Momohara, Iwao Yoshioka, Kouzou Suto, Norio Nonomura, Akihiko Okuyama, Toshifumi TakaoAbstract:CAlcium oxAlAte kidney stones contAin low Amounts of proteins, some of which hAve been implicAted in progression or prevention of kidney stone formAtion. To gAin insights into the pAthophysiology of urolithiAsis, we hAve chArActerized protein components of cAlcium oxAlAte kidney stones by proteomic ApproAches. Proteins extrActed from kidney stones showed highly heterogeneous migrAtion pAtterns in gel electrophoresis As reported. This wAs likely to be mAinly due to proteolytic degrAdAtion And protein-protein crosslinking of TAmm-HorsfAll protein And prothrombin. Protein profiles of cAlcium oxAlAte kidney stones were obtAined by in-solution proteAse digestion followed by nAnoLC-MALDI-tAndem mAss spectrometry, which resulted in identificAtion of A totAl of 92 proteins in stones from 9 urolithiAsis pAtients. Further AnAlysis showed thAt protein species And their relAtive Amounts were highly vAriAble Among individuAl stones. Although proteins such As prothrombin, osteopontin, CAlgrAnulin A And CAlgrAnulin B were found in most stones tested, some sAmples hAd high contents of prothrombin And osteopontin, while others hAd high contents of CAlgrAnulins. In Addition, CAlgrAnulin-rich stones hAd vArious neutrophil-enriched proteins such As myeloperoxidAse And lActotrAnsferrin. These proteomic profiles of individuAl kidney stones suggest thAt multiple systems composed of different groups of proteins including leucocyte
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Diversity in protein profiles of individuAl cAlcium oxAlAte kidney stones.
PloS one, 2013Co-Authors: Nobuaki Okumura, Masao Tsujihata, Chikahiro Momohara, Iwao Yoshioka, Kouzou Suto, Norio Nonomura, Akihiko Okuyama, Toshifumi TakaoAbstract:CAlcium oxAlAte kidney stones contAin low Amounts of proteins, some of which hAve been implicAted in progression or prevention of kidney stone formAtion. To gAin insights into the pAthophysiology of urolithiAsis, we hAve chArActerized protein components of cAlcium oxAlAte kidney stones by proteomic ApproAches. Proteins extrActed from kidney stones showed highly heterogeneous migrAtion pAtterns in gel electrophoresis As reported. This wAs likely to be mAinly due to proteolytic degrAdAtion And protein-protein crosslinking of TAmm-HorsfAll protein And prothrombin. Protein profiles of cAlcium oxAlAte kidney stones were obtAined by in-solution proteAse digestion followed by nAnoLC-MALDI-tAndem mAss spectrometry, which resulted in identificAtion of A totAl of 92 proteins in stones from 9 urolithiAsis pAtients. Further AnAlysis showed thAt protein species And their relAtive Amounts were highly vAriAble Among individuAl stones. Although proteins such As prothrombin, osteopontin, CAlgrAnulin A And CAlgrAnulin B were found in most stones tested, some sAmples hAd high contents of prothrombin And osteopontin, while others hAd high contents of CAlgrAnulins. In Addition, CAlgrAnulin-rich stones hAd vArious neutrophil-enriched proteins such As myeloperoxidAse And lActotrAnsferrin. These proteomic profiles of individuAl kidney stones suggest thAt multiple systems composed of different groups of proteins including leucocyte-derived ones Are differently involved in pAthogenesis of individuAl kidney stones depending on situAtions.
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Western blot AnAlysis of mAjor proteins in CAOx kidney stones.
2013Co-Authors: Nobuaki Okumura, Masao Tsujihata, Chikahiro Momohara, Iwao Yoshioka, Kouzou Suto, Norio Nonomura, Akihiko Okuyama, Toshifumi TakaoAbstract:ExtrActs of CAOx kidney stones contAining 0.1 µg proteins were sepArAted by SDS-PAGE And blotted on A PVDF membrAne. To confirm the reActivity of Antibodies And indicAte the size of the proteins in urine, A concentrAted urine sAmple from A normAl subject (1 µg protein) wAs Applied on the lAst lAne of eAch gel. The membrAne wAs then probed with Anti-prothrombin frAgment 1, Anti-CAlgrAnulin A, Anti-CAlgrAnulin B or Anti-THP Antibodies. Arrows indicAte the positions of prothrombin frAgment 1 (upper left), full length THP (upper right), full length CAlgrAnulin A (lower left), And full length CAlgrAnulin B (lower right). Western blotting wAs repeAted two times And gAve similAr results. When SAmple 1, 3, 9 And 7 (Group 1) wAs compAred with SAmple 8, 6, 2 And 5 (Group 2), p-vAlue of MAnn-Whitney U-test wAs 0.028 for prothrombin, CAlgrAnulin A And CAlgrAnulin B, while thAt for THP wAs 0.8857.
Nobuaki Okumura - One of the best experts on this subject based on the ideXlab platform.
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Diversity in Protein Profiles of IndividuAl CAlcium OxAlAte Kidney Stones
2016Co-Authors: Nobuaki Okumura, Masao Tsujihata, Chikahiro Momohara, Iwao Yoshioka, Kouzou Suto, Norio Nonomura, Akihiko Okuyama, Toshifumi TakaoAbstract:CAlcium oxAlAte kidney stones contAin low Amounts of proteins, some of which hAve been implicAted in progression or prevention of kidney stone formAtion. To gAin insights into the pAthophysiology of urolithiAsis, we hAve chArActerized protein components of cAlcium oxAlAte kidney stones by proteomic ApproAches. Proteins extrActed from kidney stones showed highly heterogeneous migrAtion pAtterns in gel electrophoresis As reported. This wAs likely to be mAinly due to proteolytic degrAdAtion And protein-protein crosslinking of TAmm-HorsfAll protein And prothrombin. Protein profiles of cAlcium oxAlAte kidney stones were obtAined by in-solution proteAse digestion followed by nAnoLC-MALDI-tAndem mAss spectrometry, which resulted in identificAtion of A totAl of 92 proteins in stones from 9 urolithiAsis pAtients. Further AnAlysis showed thAt protein species And their relAtive Amounts were highly vAriAble Among individuAl stones. Although proteins such As prothrombin, osteopontin, CAlgrAnulin A And CAlgrAnulin B were found in most stones tested, some sAmples hAd high contents of prothrombin And osteopontin, while others hAd high contents of CAlgrAnulins. In Addition, CAlgrAnulin-rich stones hAd vArious neutrophil-enriched proteins such As myeloperoxidAse And lActotrAnsferrin. These proteomic profiles of individuAl kidney stones suggest thAt multiple systems composed of different groups of proteins including leucocyte
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Diversity in protein profiles of individuAl cAlcium oxAlAte kidney stones.
PloS one, 2013Co-Authors: Nobuaki Okumura, Masao Tsujihata, Chikahiro Momohara, Iwao Yoshioka, Kouzou Suto, Norio Nonomura, Akihiko Okuyama, Toshifumi TakaoAbstract:CAlcium oxAlAte kidney stones contAin low Amounts of proteins, some of which hAve been implicAted in progression or prevention of kidney stone formAtion. To gAin insights into the pAthophysiology of urolithiAsis, we hAve chArActerized protein components of cAlcium oxAlAte kidney stones by proteomic ApproAches. Proteins extrActed from kidney stones showed highly heterogeneous migrAtion pAtterns in gel electrophoresis As reported. This wAs likely to be mAinly due to proteolytic degrAdAtion And protein-protein crosslinking of TAmm-HorsfAll protein And prothrombin. Protein profiles of cAlcium oxAlAte kidney stones were obtAined by in-solution proteAse digestion followed by nAnoLC-MALDI-tAndem mAss spectrometry, which resulted in identificAtion of A totAl of 92 proteins in stones from 9 urolithiAsis pAtients. Further AnAlysis showed thAt protein species And their relAtive Amounts were highly vAriAble Among individuAl stones. Although proteins such As prothrombin, osteopontin, CAlgrAnulin A And CAlgrAnulin B were found in most stones tested, some sAmples hAd high contents of prothrombin And osteopontin, while others hAd high contents of CAlgrAnulins. In Addition, CAlgrAnulin-rich stones hAd vArious neutrophil-enriched proteins such As myeloperoxidAse And lActotrAnsferrin. These proteomic profiles of individuAl kidney stones suggest thAt multiple systems composed of different groups of proteins including leucocyte-derived ones Are differently involved in pAthogenesis of individuAl kidney stones depending on situAtions.
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Western blot AnAlysis of mAjor proteins in CAOx kidney stones.
2013Co-Authors: Nobuaki Okumura, Masao Tsujihata, Chikahiro Momohara, Iwao Yoshioka, Kouzou Suto, Norio Nonomura, Akihiko Okuyama, Toshifumi TakaoAbstract:ExtrActs of CAOx kidney stones contAining 0.1 µg proteins were sepArAted by SDS-PAGE And blotted on A PVDF membrAne. To confirm the reActivity of Antibodies And indicAte the size of the proteins in urine, A concentrAted urine sAmple from A normAl subject (1 µg protein) wAs Applied on the lAst lAne of eAch gel. The membrAne wAs then probed with Anti-prothrombin frAgment 1, Anti-CAlgrAnulin A, Anti-CAlgrAnulin B or Anti-THP Antibodies. Arrows indicAte the positions of prothrombin frAgment 1 (upper left), full length THP (upper right), full length CAlgrAnulin A (lower left), And full length CAlgrAnulin B (lower right). Western blotting wAs repeAted two times And gAve similAr results. When SAmple 1, 3, 9 And 7 (Group 1) wAs compAred with SAmple 8, 6, 2 And 5 (Group 2), p-vAlue of MAnn-Whitney U-test wAs 0.028 for prothrombin, CAlgrAnulin A And CAlgrAnulin B, while thAt for THP wAs 0.8857.
Alexander D. Romaschin - One of the best experts on this subject based on the ideXlab platform.
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A strAtegy for high resolution protein identificAtion in surfAce enhAnced lAser desorption ionizAtion mAss spectrometry CAlgrAnulin A And chAperonin 10 As protein mArkers for endometriAl cArcinomA
Proteomics, 2005Co-Authors: Jingzhong Guo, Eric C.c. Yang, Leroi V. Desouza, Georg Diehl, Mary Joe Rodrigues, Alexander D. Romaschin, Terence J. Colgan, K Michael W SiuAbstract:SurfAce-enhAnced lAser desorption/ionizAtion-mAss spectrometry (SELDI-MS) hAs conventionAlly been prActiced on lineAr time of flight (TOF) which hAs low mAss AccurAcy And resolution. Here we demonstrAte in An exAminAtion of both mAlignAnt And nonmAlignAnt endometriAl tissue homogenAtes thAt high mAss AccurAcy And resolution in the MS stAge Are cruciAl. Using A commerciAlly AvAilAble quAdrupole/TOF (QqTOF), we were Able to resolve two potentiAl cAncer mArkers, subsequently identified off-line As chAperonin 10 And CAlgrAnulin A, thAt differ by 8 DA in mAss. Two off-line protein identificAtion protocols were developed: the first wAs bAsed on size-exclusion chromAtogrAphy (SEC), sodium dodecyl sulfAte-polyAcrylAmide gel electrophoresis (SDS-PAGE), protein extrAction, trypsin digestion, And mAtrix-Assisted lAser desorption/ionizAtion-tAndem MS (MALDI-MS/MS); the second on SEC And shotgun nAno-liquid chromAtogrAphy (nAnoLC)-MS/MS. AnAlyses on A cohort of 44 endometriAl homogenAtes showed 22 out of 23 nonmAlignAnt sAmples hAd nondetectAble to very low AbundAnce of chAperonin 10 And CAlgrAnulin A; 17 of the 21 mAlignAnt sAmples hAd detectAble to AbundAnt levels of both proteins. ImmunohistochemicAl stAining of A tissue microArrAy of 32 sAmples showed thAt ApproximAtely hAlf of mAlignAnt endometriAl tissues exhibited positive stAining for CAlgrAnulin A in the mAlignAnt epithelium, while 9 out of 10 benign tissues exhibited negAtive epitheliAl stAining. In Addition, mAcrophAges/grAnulocytes in mAlignAnt As well As nonmAlignAnt tissues showed positive stAining. No immunostAining occurred in stromA or myometrium. CAlgrAnulin A, in combinAtion with chAperonin 10 And other proteins, mAy eventuAlly constitute A pAnel of mArkers to permit diAgnosis And screening of endometriAl cAncer.
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A strAtegy for high‐resolution protein identificAtion in surfAce‐enhAnced lAser desorption/ionizAtion mAss spectrometry: CAlgrAnulin A And chAperonin 10 As protein mArkers for endometriAl cArcinomA
Proteomics, 2005Co-Authors: Jingzhong Guo, Eric C.c. Yang, Leroi V. Desouza, Georg Diehl, Mary Joe Rodrigues, Alexander D. Romaschin, Terence J. Colgan, K. W. Michael SiuAbstract:SurfAce-enhAnced lAser desorption/ionizAtion-mAss spectrometry (SELDI-MS) hAs conventionAlly been prActiced on lineAr time of flight (TOF) which hAs low mAss AccurAcy And resolution. Here we demonstrAte in An exAminAtion of both mAlignAnt And nonmAlignAnt endometriAl tissue homogenAtes thAt high mAss AccurAcy And resolution in the MS stAge Are cruciAl. Using A commerciAlly AvAilAble quAdrupole/TOF (QqTOF), we were Able to resolve two potentiAl cAncer mArkers, subsequently identified off-line As chAperonin 10 And CAlgrAnulin A, thAt differ by 8 DA in mAss. Two off-line protein identificAtion protocols were developed: the first wAs bAsed on size-exclusion chromAtogrAphy (SEC), sodium dodecyl sulfAte-polyAcrylAmide gel electrophoresis (SDS-PAGE), protein extrAction, trypsin digestion, And mAtrix-Assisted lAser desorption/ionizAtion-tAndem MS (MALDI-MS/MS); the second on SEC And shotgun nAno-liquid chromAtogrAphy (nAnoLC)-MS/MS. AnAlyses on A cohort of 44 endometriAl homogenAtes showed 22 out of 23 nonmAlignAnt sAmples hAd nondetectAble to very low AbundAnce of chAperonin 10 And CAlgrAnulin A; 17 of the 21 mAlignAnt sAmples hAd detectAble to AbundAnt levels of both proteins. ImmunohistochemicAl stAining of A tissue microArrAy of 32 sAmples showed thAt ApproximAtely hAlf of mAlignAnt endometriAl tissues exhibited positive stAining for CAlgrAnulin A in the mAlignAnt epithelium, while 9 out of 10 benign tissues exhibited negAtive epitheliAl stAining. In Addition, mAcrophAges/grAnulocytes in mAlignAnt As well As nonmAlignAnt tissues showed positive stAining. No immunostAining occurred in stromA or myometrium. CAlgrAnulin A, in combinAtion with chAperonin 10 And other proteins, mAy eventuAlly constitute A pAnel of mArkers to permit diAgnosis And screening of endometriAl cAncer.
Terence J. Colgan - One of the best experts on this subject based on the ideXlab platform.
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A strAtegy for high resolution protein identificAtion in surfAce enhAnced lAser desorption ionizAtion mAss spectrometry CAlgrAnulin A And chAperonin 10 As protein mArkers for endometriAl cArcinomA
Proteomics, 2005Co-Authors: Jingzhong Guo, Eric C.c. Yang, Leroi V. Desouza, Georg Diehl, Mary Joe Rodrigues, Alexander D. Romaschin, Terence J. Colgan, K Michael W SiuAbstract:SurfAce-enhAnced lAser desorption/ionizAtion-mAss spectrometry (SELDI-MS) hAs conventionAlly been prActiced on lineAr time of flight (TOF) which hAs low mAss AccurAcy And resolution. Here we demonstrAte in An exAminAtion of both mAlignAnt And nonmAlignAnt endometriAl tissue homogenAtes thAt high mAss AccurAcy And resolution in the MS stAge Are cruciAl. Using A commerciAlly AvAilAble quAdrupole/TOF (QqTOF), we were Able to resolve two potentiAl cAncer mArkers, subsequently identified off-line As chAperonin 10 And CAlgrAnulin A, thAt differ by 8 DA in mAss. Two off-line protein identificAtion protocols were developed: the first wAs bAsed on size-exclusion chromAtogrAphy (SEC), sodium dodecyl sulfAte-polyAcrylAmide gel electrophoresis (SDS-PAGE), protein extrAction, trypsin digestion, And mAtrix-Assisted lAser desorption/ionizAtion-tAndem MS (MALDI-MS/MS); the second on SEC And shotgun nAno-liquid chromAtogrAphy (nAnoLC)-MS/MS. AnAlyses on A cohort of 44 endometriAl homogenAtes showed 22 out of 23 nonmAlignAnt sAmples hAd nondetectAble to very low AbundAnce of chAperonin 10 And CAlgrAnulin A; 17 of the 21 mAlignAnt sAmples hAd detectAble to AbundAnt levels of both proteins. ImmunohistochemicAl stAining of A tissue microArrAy of 32 sAmples showed thAt ApproximAtely hAlf of mAlignAnt endometriAl tissues exhibited positive stAining for CAlgrAnulin A in the mAlignAnt epithelium, while 9 out of 10 benign tissues exhibited negAtive epitheliAl stAining. In Addition, mAcrophAges/grAnulocytes in mAlignAnt As well As nonmAlignAnt tissues showed positive stAining. No immunostAining occurred in stromA or myometrium. CAlgrAnulin A, in combinAtion with chAperonin 10 And other proteins, mAy eventuAlly constitute A pAnel of mArkers to permit diAgnosis And screening of endometriAl cAncer.
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A strAtegy for high‐resolution protein identificAtion in surfAce‐enhAnced lAser desorption/ionizAtion mAss spectrometry: CAlgrAnulin A And chAperonin 10 As protein mArkers for endometriAl cArcinomA
Proteomics, 2005Co-Authors: Jingzhong Guo, Eric C.c. Yang, Leroi V. Desouza, Georg Diehl, Mary Joe Rodrigues, Alexander D. Romaschin, Terence J. Colgan, K. W. Michael SiuAbstract:SurfAce-enhAnced lAser desorption/ionizAtion-mAss spectrometry (SELDI-MS) hAs conventionAlly been prActiced on lineAr time of flight (TOF) which hAs low mAss AccurAcy And resolution. Here we demonstrAte in An exAminAtion of both mAlignAnt And nonmAlignAnt endometriAl tissue homogenAtes thAt high mAss AccurAcy And resolution in the MS stAge Are cruciAl. Using A commerciAlly AvAilAble quAdrupole/TOF (QqTOF), we were Able to resolve two potentiAl cAncer mArkers, subsequently identified off-line As chAperonin 10 And CAlgrAnulin A, thAt differ by 8 DA in mAss. Two off-line protein identificAtion protocols were developed: the first wAs bAsed on size-exclusion chromAtogrAphy (SEC), sodium dodecyl sulfAte-polyAcrylAmide gel electrophoresis (SDS-PAGE), protein extrAction, trypsin digestion, And mAtrix-Assisted lAser desorption/ionizAtion-tAndem MS (MALDI-MS/MS); the second on SEC And shotgun nAno-liquid chromAtogrAphy (nAnoLC)-MS/MS. AnAlyses on A cohort of 44 endometriAl homogenAtes showed 22 out of 23 nonmAlignAnt sAmples hAd nondetectAble to very low AbundAnce of chAperonin 10 And CAlgrAnulin A; 17 of the 21 mAlignAnt sAmples hAd detectAble to AbundAnt levels of both proteins. ImmunohistochemicAl stAining of A tissue microArrAy of 32 sAmples showed thAt ApproximAtely hAlf of mAlignAnt endometriAl tissues exhibited positive stAining for CAlgrAnulin A in the mAlignAnt epithelium, while 9 out of 10 benign tissues exhibited negAtive epitheliAl stAining. In Addition, mAcrophAges/grAnulocytes in mAlignAnt As well As nonmAlignAnt tissues showed positive stAining. No immunostAining occurred in stromA or myometrium. CAlgrAnulin A, in combinAtion with chAperonin 10 And other proteins, mAy eventuAlly constitute A pAnel of mArkers to permit diAgnosis And screening of endometriAl cAncer.
