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Protamine P1
Symbol Protamine_P1
Pfam PF00260
InterPro IPR000221
protamine 1
Symbol PRM1
Entrez 5619
HUGO 9447
OMIM 182880
RefSeq NM_002761
UniProt P04553
Other data
Locus Chr. 16 p13.13
protamine 2
Symbol PRM2
Entrez 5620
HUGO 9448
OMIM 182890
RefSeq NM_002762
UniProt P04554
Other data
Locus Chr. 16 p13.13

Protamines are small, arginine-rich, nuclear proteins that replace histones late in the haploid phase of spermatogenesis and are believed essential for sperm head condensation and DNA stabilization. They may allow for denser packaging of DNA in spermatozoon than histones, but they must be decompressed before the genetic data can be used for protein synthesis. However, in humans and maybe other primates, 10-15% of the sperm's genome is packaged by histones thought to bind genes that are essential for early embryonic development.[1]

Medical uses[edit]

When mixed with insulin, protamines slow down the onset and increase the duration of insulin action (see NPH insulin).[2]

Protamine is used in cardiac surgery, vascular surgery, and interventional radiology procedures to neutralize the anti-clotting effects of heparin. Adverse effects include increased pulmonary artery pressure and decrease peripheral blood pressure, myocardial oxygen consumption, cardiac output, and heart rate.[3]

Protamine sulfate is an antidote for heparin overdose.[4] A chain shortened version of protamine also acts as a potent heparin antagonist, but with markedly reduced antigenicity.[5]

In gene therapy, protamine sulfate's ability to condense plasmid DNA along with its approval by the U.S. Food and Drug Administration (FDA) have made it an appealing candidate to increase transduction rates by both viral[6] and nonviral (e.g. utilizing cationic liposomes)[7] mediated delivery mechanisms.


Mice, humans, rat [8] and certain fish have two or more different protamines, whereas the sperm of bull and boar,[9] have one form of protamine due to a mutation in the PRM2 gene.


The 2 human protamines are denoted PRM1 and PRM2.


Examples of protamines from fish are:

Protamine structure[edit]

The secondary and tertiary structure of protamine is not known with certainty, but several proposals have been published.[10][11][12]


  1. ^ Balhorn R (2007). "The protamine family of sperm nuclear proteins". Genome Biol 8 (9): 227. doi:10.1186/gb-2007-8-9-227. PMC 2375014. PMID 17903313. 
  2. ^ Owens DR (June 2011). "Insulin preparations with prolonged effect". Diabetes Technol. Ther. 13 Suppl 1: S5–14. doi:10.1089/dia.2011.0068. PMID 21668337. 
  3. ^ Carr JA, Silverman N (1999). "The heparin-protamine interaction. A review.". J Cardiovasc Surg (Torino) 40 (5): 659–66. PMID 10596998. 
  4. ^ Weiler JM, Freiman P, Sharath MD, Metzger WJ, Smith JM, Richerson HB et al. (1985). "Serious adverse reactions to protamine sulfate: are alternatives needed?". J Allergy Clin Immunol 75 (2): 297–303. doi:10.1016/0091-6749(85)90061-2. PMID 2857186. 
  5. ^ Byun Y, Chang LC, Lee LM, Han IS, Singh VK, Yang VC (2000). "Low molecular weight protamine: a potent but nontoxic antagonist to heparin/low molecular weight protamine". Asaio J. 46 (4): 435–9. doi:10.1097/00002480-200007000-00013. PMID 10926141. 
  6. ^ Kenneth Cornetta, W.French Anderson (1989). "Protamine sulfate as an effective alternative to polybrene in retroviral-mediated gene-transfer: implications for human gene therapy". Journal of Virological Methods 23 (2): 187–194. doi:10.1016/0166-0934(89)90132-8. PMID 2786000. 
  7. ^ Sorgi, FL; Bhattacharya, S; Huang, L (Sep 1997). "Protamine sulfate enhances lipid-mediated gene transfer." (PDF). Gene therapy 4 (9): 961–8. doi:10.1038/ PMID 9349433. 
  8. ^ (PDF)  Missing or empty |title= (help)
  9. ^  Missing or empty |title= (help)
  10. ^ Martins RP, Ostermeier GC, Krawetz SA (December 2004). "Nuclear matrix interactions at the human protamine domain: a working model of potentiation". J. Biol. Chem. 279 (50): 51862–8. doi:10.1074/jbc.M409415200. PMID 15452126. 
  11. ^ Vilfan ID, Conwell CC, Hud NV (May 2004). "Formation of native-like mammalian sperm cell chromatin with folded bull protamine". J. Biol. Chem. 279 (19): 20088–95. doi:10.1074/jbc.M312777200. PMID 14990583. 
  12. ^ Biegeleisen K (August 2006). "The probable structure of the protamine-DNA complex". J. Theor. Biol. 241 (3): 533–40. doi:10.1016/j.jtbi.2005.12.015. PMID 16442565. 

External links[edit]