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International Institute of Molecular and Cell Biology
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About IIMCB Authorities
Jacek Kuznicki

b. 1952; M Sc in biochemistry; Warsaw University, 1976; PhD in biochemistry, Nencki Institute, 1980; post-doctoral 1981-1984, NIH, Bethesda, MD, USA; 1986-2002, head of the laboratory, Nencki Institute; habilitation 1987; Scientific Director at the Nencki Institute 1990-1992; Secretary of the Polish Biochemical Society, 1989-1992; Full Professor 1993, Member of Polish Academy of Sciences, 2004; Co-Editor of “Advances in Biochemistry” (in Polish), 1989-1992; Visiting Professor 1992-1995, NIMH, Bethesda, MD, USA; Member of Advisory Boards of Biochem J and Acta Biochem Pol, Acting Director at International Institute of Molecular and Cell Biology in Warsaw 1998-2001, Director of Center of Excellence for Studies on Mechanisms of Neurodegeneration located at the Nencki Institute, November 1999-2000; Director of Polish Centenarian Program 1999-present), Director at International Institute of Molecular and Cell Biology in Warsaw 2002-present.

Current research interests:

  • Alzheimer disease and other neurodegenerative disases
  • Aging and longevity
  • Protein structure-function analysis
  • Calcium regulation and homeostasis
  • Calcium-binding proteins
  • Cell specific gene expression

Chief achievements:

  • Characterization of calcium-dependent conformational changes of calmodulin, its distribution, and discovery of calmodulin in Protozoa (1976-1981),
  • Presenting evidence for supramolecular regulation of actin-activated myosin II ATPase from Acanthamoeba castellani (1982-1984),
  • Discovery, purification, and characterization of calcyclin (S100A6) (1985-1992),
  • Presenting evidence for calcium dependent conformational changes of calretinin (1993-1996),
  • Discovery and characterization of a novel brain protein involved in ubiquitination (CacyBP/SIP)(1993-2005),
  • Description of mechanisms involved in expression of calcyclin gene 1996-2006),
  • Organization of the Polish Centenarians Program (1998-2002),
  • Characterization of calretinin I-II domain (1998-2005),
  • Identification of novel FAD and FTD mutations in presenilins (2003-2006),
  • Characterization of Sgt1 protein, homolog of CacyBP/SIP (2003-2006),
  • Characterization of calmyrin and its protein partners (2005-2006),
  • Supervisor of 7 Ph.D. theses defended in 1990, 1992, 1995, 2001, 2002(2x), 2003.

Author of (87) articles cited by Medline and published in J Biol Chem (9 papers), FEBS Lett (6), Biochim Biophys Acta (10), J Neurochem (3), Biochem J (3), Biochemistry (3), Prot Exp Purif (2), Eur J Biochem (2), Prot Sci (2), Neurochem Int, Exp Neurol (2), J Cell Biochem,
J Neural Trans, Neurosci Lett (2), Int J Biochem (4), Cancer Res, Exp Cell Res, NeuroReport, Eur J Cancer, Mol Brain Res, J Histochem Cytochem, and other.

Selected publications since 1995:

Larson-Thome K, Weberg L, Szybinska A, Mossakowska M, Barcikowska M, Styczynska M, Zekanowski C, Kuznicki J, Erickson RP (2008) Variation in NPC1 gene, encoding Niemann-Pick C1 protein involved in intracellular cholesterol transport, is associated with Alzheimer disease. Neurosci Lett. (in press)

Bojarski L, Herms J, Kuznicki J (2008) Calcium dysregulation in Alzheimer's disease. Neurochemistry Int, 52, 621-633

Wojda U, Salinska E, Kuznicki J (2008) Calcium ions in neuronal degeneration. IUBMB Life, Sep;60(9):575-90

Filipek A, Michowski W, Kuznicki J (2008) Involvement of S100A6 (calcyclin) and its binding partners in intracellular signaling pathways. Advan. Enzyme Regul. 48, 225-239

Lanni C, Racchi M, Mazzini G, Ranzenigo A, Polotti R, Sinforiani E, Olivari L, Barcikowska M, Styczynska M, Kuznicki J, Szybinska A, Govoni S, Memo M, Uberti D (2008) Conformationally altered p53: a novel Alzheimer's disease marker? Mol Psychiatry, 13(6):641-7

Zabka M, Lesniak W, Prus W, Kuznicki J, Filipek A (2008) Sgt1 has co-chaperone properties and is up-regulated by heat shock. Biochem Biophys Res Commun. 370(1):179-83

Schneider G, Nieznanski K, Kilanczyk E, Bieganowski P, Kuznicki J, Filipek A. (2007) CacyBP/SIP interacts with tubulin in neuroblastoma NB2a cells and induces formation of globular tubulin assemblies. BBA-Molecular Cell Research, 2007 Nov; 1773(11):1628-36

Bojarski L, Lewandowicz A, Blazejczyk M, Sobczak A, Kuznicki J, Wojda U (2007) Biochemical properties of endogenous presenilin 1 and presenilin 2 in cultured human B-lymphocytes. Clin Chem Lab Med. 45(10):1273-6

Lesniak W, Slomnicki LP, Kuznicki J (2007) Epigenetic Control of the S100A6 (Calcyclin) Gene Expression. J Invest Derm, 127:2307-14

Wollmer MA, Sleegers K, Ingelsson M, Zekanowski C, Brouwers N, Maruszak A, Brunner F, Huynh KD, Kilander L, Brundin RM, Hedlund M, Giedraitis V, Glaser A, Engelborghs S, De Deyn PP, Kapaki E, Tsolaki M, Daniilidou M, Molyva D, Paraskevas GP, Thal DR, Barcikowska M, Kuznicki J, Lannfelt L, Van Broeckhoven C, Nitsch RM, Hock C, Papassotiropoulos A (2007) Association study of cholesterol-related genes in Alzheimer's disease.
Neurogenetics, 8(3):179-88

Spiechowicz M, Zylicz A, Bieganowski P, Kuznicki J, Filipek A (2007) Hsp70 is a new target of Sgt1-an interaction modulated by S100A6. Biochem Biophys Res Commun, 357(4):1148-53

Spiechowicz M, Bernstein HG, Dobrowolny H, Lesniak W, Mawrin C, Bogerts B, Kuznicki J, Filipek A (2006) Density of Sgt1-immunopositive neurons is decreased in the cerebral cortex of Alzheimer's disease brain. Neurochem Int. 49(5):487-93

Blazejczyk M, Wojda U, Sobczak A, Spilker C, Bernstein HG, Gundelfinger ED, Kreutz MR, Kuznicki J (2006) Ca2+-independent binding and cellular expression profiles question a significant role of calmyrin in transduction of Ca2+-signals to Alzheimer's disease-related presenilin 2 in forebrain. Biochim Biophys Acta. 1762(1):66-72

Zekanowski C, Golan MP, Krzysko KA, Lipczynska-Lojkowska W, Filipek S, Kowalska A, Rossa G, Peplonska B, Styczynska M, Maruszak A, Religa D, Wender M, Kulczycki J, Barcikowska M, Kuznicki J (2006) Two novel presenilin 1 gene mutations connected with frontotemporal dementia-like clinical phenotype: genetic and bioinformatic assessment. Exp Neurol. 200(1):82-8

Lesniak W, Kuznicki J (2006) Binding and functional characteristics of two E-box motifs within the S100A6 (calcyclin)gene promoter. J Cell Biochem. 97(5):1017-1024

Sobczak A, Blazejczyk M, Piszczek G, Zhao G, Kuznicki J, Wojda U (2005) Calcium-binding calmyrin forms stable covalent dimers in vitro, but in vivo is found in monomeric form. Acta Biochim Pol. 52(2):469-76

Bernstein HG, Blazejczyk M, Rudka T, Gundelfinger ED, Dobrowolny H, Bogerts B, Kreutz MR, Kuznicki J, Wojda U (2005) The Alzheimer disease-related calcium-binding protein calmyrin is prominently expressed in human forebrain with an altered distribution in Alzheimer's as compared to normal aging brains. Neuropathol Appl Neurobiol 31(3):314-24


Bhattacharya S, Lee YT, Michowski W, Jastrzebska B, Filipek A,
Kuznicki J, Chazin WJ (2005) The modular structure of SIP facilitates its role in stabilizing multiprotein assemblies. Biochemistry. 44(27):9462-71


Lesniak W, Szczepanska A,
Kuznicki J (2005) Calcyclin (S100A6) expression is stimulated by agents evoking oxidative stress via the antioxidant response element. Biochim Biophys Acta. 2005 May 15;1744(1):29-37


Palczewska M, Batta G, Groves P, Linse S,
Kuznicki J (2005) Characterization of calretinin I-II as an EF-hand, Ca2+, H+-sensing domain. Protein Sci. 2005 Jul;14(7):1879-87

Puzianowska-Kuznicka M, Kuznicki J (2005) Genetic alterations in accelerated ageing syndromes. Do they play a role in natural ageing? Int J Biochem Cell Biol. 37(5):947-60


Zekanowski C
, Religa D, Safranow K, Maruszak A, Dziedziejko V, Styczynska M, Gacia M, Golan M, Peplonska B, Chlubek D, Kuznicki J, Barcikowska M (2005) The -22c/t polymorphism in presenilin 1 gene is not connected with late-onset and early-onset familial Alzheimer's disease in Poland. J Neural Transm. 112(6):839-45

Witt M, Ziemka A, Kuznicki J (2005) International Institute of Molecular and Cell Biology in Warsaw (in Polish). Postepy Biochemii 353-6


Billing-Marczak K, Zieminska E, Lesniak W, Lazarewicz JW, Kuznicki J (2004) Calretinin gene promoter activity is differently regulated in neurons and cancer cells. Role of AP2-like cis element and zinc ions. Biochim Biophys Acta 16; 1678(1): 14-21

Lee YT, Jacob J, Michowski W, Nowotny M, Kuznicki J, Chazin WJ (2004) Human Sgt1 binds HSP90 through the CHORD-Sgt1 domain and not the tetratricopeptide repeat domain. J Biol Chem 279: 16511-16517

Zekanowski C, Peplonska B, Styczynska M, Religa D, Pfeffer A, Czyzewski K, Gabryelewicz T, Szybinska A, Kijanowska-Haladyna B, Kotapka-Minc S, Luczywek E, Barczak A, Wasiak B, Chodakowska-Zebrowska M, Przekop I, Kuznicki J, Barcikowska M (2004) The E318G substitution in PSEN1 gene is not connected with Alzheimer's disease in a large Polish cohort. Neurosci. Lett 357(3): 167-170

Zekanowski C, Religa D, Graff C, Filipek S, Kuznicki J (2004) Genetic aspects of Alzheimer’s disease. Acta Neurobiol Exp 64: 19-31

M. Nowotny, M. Spiechowicz, B. Jastrzebska, A. Filipek, K Kitagawa, J. Kuznicki (2003) Calcium-regulated interaction of Sgt1 with S100A6 (calcyclin) and other S100 proteins. J. Biol. Chem. 278(29): 26923-26928

B. Peplonska, C. Zekanowski, D. Religa, K. Czyzewski, M. Styczynska, A. Pfeffer, T. Gabryelewicz, M. Golebiowski, E. Luczywek, B. Wasiak, A. Barczak, M. Chodakowska, M. Barcikowska, J. Kuznicki (2003) Strong association between Saitohin gene polymorphism and tau haplotype in the Polish population. Neurosci. Lett. 348(3): 163-166

C. Zekanowski, M. Styczynska, B. Peplonska, T. Gabryelewicz, D. Religa, J. Ilkowski, B. Kijanowska-Haladyna, S. Kotapka-Minc, S. Mikkelsen, A. Pfeffer, A. Barczak, E. Luczywek, B. Wasiak, M. Chodakowska-Zebrowska, K. Gustaw, J. Laczkowski, T. Sobow, J. Kuznicki, M. Barcikowska (2003) Mutations in presenilin 1, presenilin 2 and amyloid precursor protein genes in patients with familial Alzheimer disease in Poland. Exp. Neurol. 184: 991-996

C. Zekanowski , B. Peplonska, M. Styczynska, K. Gustaw, J. Kuznicki, M. Barcikowska (2003) Mutation screening of the MAPT and the STH genes in Polish patients with clinically diagnosed frontotemporal dementia (FTD). Dement. Geriatr. Cogn. Disord. 16(3): 126-131


M. Palczewska, P. Groves, G. Batta, B. Heise, J. Kuznicki (2003) Calretinin and calbindin D28k have different domain organizations. Prot. Sci. 12: 180-184

K. Billing-Marczak, L. Buzanska, L. Winsky, M. Nowotny, T. Rudka, K. Isaacs, M.F. Belin, J. Kuznicki (2002) AP2-Like element is required for calretinin gene promoter activity in cells of neuronal phenotype differentiated from multipotent human cell line DEV. Biochim. Biophys. Acta 1577: 412-420

A. Filipek,B. Jastrzebska, M. Nowotny, J. Kuznicki (2002) CacyBP/SIP, a Calcyclin and Siah-1-interacting Protein, Binds EF-hand Proteins of the S100 Family. J. Biol. Chem. 277: 28848-52

A. Filipek, B. Jastrzebska, M. Nowotny, K. Kwiatkowska, M. Hetman, L. Surmacz, E. Wyroba and J. Kuznicki (2002) Ca2+-dependent translocation of the calcyclin-binding protein in Neurons and neuroblastoma NB-2a cells. J. Biol. Chem., 277: 21103-9

M. Palczewska, P. Groves, A. Ambrus, A. Kaleta, K. E. Kövér, G. Batta, J. Kuznicki (2001) Structural and biochemical characterization of neuronal calretinin domain I-II (residues 1-100); comparison to homologous calbindin D28k domain I-II (residues 1-93). Eur. J. Biochem., 268: 6229-6237

M. Nowotny, S. Bhattacharya, A. Filipek, A. M. Krezel, W. Chazin, J. Kuznicki (2000) Characterization of the interaction of calcyclin (S100A6) and calcyclin-binding protein. J. Biol. Chem. 275: 31178-31182

B. Jastrzebska, A. Filipek, D. Nowicka, L. Kaczmarek, J. Kuznicki. (2000) Calcyclin (S100A6) binding protein (CacyBP) is highly expressed in brain neurons. J. Histochem. Cytochem. 48: 1195-1202

W. Lesniak, A. Jezierska, J. Kuznicki (2000) Upstream stimulatory factor is involved in the regulation of the human calcyclin (S100A6) gene. Biochim. Biophys. Acta 1517: 73-81

M. Palczewska, P. Groves, J. Kuznicki (1999) Use of Pichia pastoris for expression, purification and characterization of rat calretinin “EF-hand” domains. Prot. Exp. Purif. 17: 465-464

K. Billing-Marczak, M. Przybyszewska, J. Kuznicki (1999) Measurements of [Ca2+] using fura-2 in glioma C6 cells expressing calretinin with GFP as a marker of transfection: no Ca2+-buffering provided by calretinin. Biochem. Biophys. Acta 1449: 169-177

A. Filipek, J. Kuznicki (1998) Molecular cloning and expression of a mouse brain cDNA encoding a novel protein target of calcyclin. J. Neurochem. 70: 1793-1798

P. Groves, B.E. Finn, J. Kuznicki, S. Forsen (1998) A model for target protein binding to calcium-activated S100 dimers. FEBS Lett. 421: 175-179

K.I. Strauss, J. Kuznicki, L. Winsky, M. Hammer, D.M. Jacobowitz (1996) The mouse calretinin gene promoter region: structural and functional components. Mol. Brain. Res. 49: 175-187

J. Kuznicki, K. R. Isaacs, D.M. Jacobowitz (1996) The expression of calretinin in transfected PC12 cells provides no protection against Ca2+-overload or trophic factors deprivation. Biochem. Biophys. Acta 1313: 194-200

J. Kuznicki (1996) Calcyclin. In: Guidebook to the Calcium-binding Proteins, (ed. MR Celio). A Sambrook & Tooze Publication at Oxford University Press, 143-145

L. Winsky and J. Kuznicki (1996) Antibody recognition of calcium-binding proteins depends on their calcium-binding status. J. Neurochem. 66: 764-771

J. Kuznicki, K.J. Strauss and D.J. Jacobowitz (1995) Conformational changes and calcium binding by calretinin and its recombinant fragments containing different sets of EF-hand motifs. Biochemistry 34: 15389-15394

J. Kuznicki, T.-C. L. Wang, B.M. Martin, L. Winsky, D.M. Jacobowitz (1995) Localization of Ca2+- dependent conformational changes of calretinin by limited tryptic proteolysis. Biochem. J. 308: 607-612

G.P. Tonini, G. Fabretti, J. Kuznicki, L. Massimo, P. Scaruffi, M. Brisigotti, (1995) Gene expression and protein localization of calcyclin, a calcium-binding protein of the S-100 family in fresh neuroblastomas. Eur. J. Cancer 31A: 499-504

L. Winsky and J. Kuznicki (1995) Distribution of calretinin, calbindin D28k, and parvalbumin in subcellular fractions of rat cerebellum: effects of calcium. J. Neurochem. 65: 381-388.

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