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µ¿¹°¼º MucinÀÌ ¿ë¾×»óÅÂ¿Í HydroxyapatiteÇ¥¸é¿¡¼­ Peroxidase È°¼º¿¡ ¹ÌÄ¡´Â ¿µÇâ¿¡ °üÇÑ ¿¬±¸

Influences of Animal Mucins on Peroxidase Activity in Solution and on the Surface of Hydroxyapatite

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À̻󱸠( Lee Sang-Goo ) - ¼­¿ï´ëÇб³ Ä¡°ú´ëÇÐ ±¸°­³»°úÁø´ÜÇб³½Ç
ÀüÀºÇü ( Jeon Eun-Hyoung ) - ¼­¿ï´ëÇб³ Ä¡°ú´ëÇÐ ±¸°­³»°úÁø´ÜÇб³½Ç
°íÈ«¼· ( Kho Hong-Seop ) - ¼­¿ï´ëÇб³ Ä¡°ú´ëÇÐ ±¸°­³»°úÁø´ÜÇб³½Ç

Abstract

µ¿¹°¼º mucinÀº ÀÎü Ÿ¾× mucin°ú À¯»çÇÑ ±¸Á¶Àû Ư¼ºÀ» °¡Áö°í ÀÖÀ¸¹Ç·Î È¿°úÀûÀΠŸ¾×´ëüÁ¦ÀÇ °³¹ß¿¡ ÀûÇÕÇÑ ¼ººÐÀ¸·Î ¿©°ÜÁ® ¿Ô´Ù. ±¸°­°ÇÁ¶Áõ ȯÀÚ°¡ µ¿¹°¼º mucin ÇÔÀ¯ Ÿ¾×´ëüÁ¦¸¦ »ç¿ëÇÒ °æ¿ì, µ¿¹°¼º mucin°ú ÀÎü Ÿ¾×¿¡ Á¸ÀçÇÏ´Â Ç×±Õ ´Ü¹éÁúÀÌ ¿ë¾×»óÅÂÀÎ ÀüŸ¾×°ú ±¸°­Ç¥¸é¿¡ Çü¼ºµÈ pellicle¿¡ µ¿½Ã¿¡ Á¸ÀçÇÒ ¼ö ÀÖÀ¸¹Ç·Î ÀÌµé ¹°Áú»çÀÌ¿¡ »óÈ£ÀÛ¿ëÀÌ ÀÏ¾î ³¯ ¼ö ÀÖÀ» °ÍÀÌ´Ù. º» ¿¬±¸ÀÇ ¸ñÀûÀº ¿ë¾×°ú hydroxyapatite (HA) Ç¥¸é¿¡¼­ µ¿¹°¼º mucinÀÌ peroxidase È°¼º¿¡ ¹ÌÄ¡´Â ¿µÇâÀ» Æò°¡Çϱâ À§ÇÏ¿© ½ÃÇàµÇ¾ú´Ù. µ¿¹°¼º mucinÀÌ peroxidase È°¼º¿¡ ¹ÌÄ¡´Â ¿µÇâÀº µÅÁöÀÇ À§Àå mucin (porcine gastric mucin, PGM) À̳ª ¼ÒÀÇ ¾ÇÇϼ± mucin (bovine submaxillary mucin, BSM)À» ¼ÒÀÇ lactoperoxidase (bovine lactoperoxidase, bLPO)³ª Ÿ¾×°Ëü¿Í incubationÇÏ´Â ¹æ¹ýÀ» »ç¿ëÇÏ¿© ºÐ¼®ÇÏ¿´°í, Ç¥¸é»óÅ¿¡¼­ÀÇ ¿¬±¸¸¦ À§ÇØ HA beads, HA disc, ¼ÒÀÇ Ä¡¾Æ¿Í °°Àº 3°¡Áö Á¾·ùÀÇ HA Ç¥¸éÀ» È°¿ëÇÏ¿´´Ù. Peroxidase È°¼ºÀº NbsSCN ¹ýÀ» ÀÌ¿ëÇÏ¿© ºÐ¼®ÇÏ¿´´Ù.
1. µÅÁöÀ§Àå mucinÀº ¿ë¾×»óÅ¿¡¼­ bLPO È°¼ºÀ» Áõ°¡½ÃÄ×À¸³ª Ÿ¾×°ËüÀÇ peroxidase (peroxidase in saliva sample, POS) È°¼º¿¡´Â ¿µÇâÀ» ¹ÌÄ¡Áö ¾Ê¾Ò´Ù.
2. ¼Ò ¾ÇÇϼ± mucinÀº ¿ë¾×»óÅ¿¡¼­ bLPO¿Í POS È°¼º¿¡ ¿µÇâÀ» ¹ÌÄ¡Áö ¾Ê¾Ò´Ù.
3. HA Ç¥¸é¿¡ ºÎÂøµÈ µÅÁöÀ§Àå mucinÀº peroxidaseÀÇ ºÎÂø°ú È°¼ºÀ» Áõ°¡½ÃÄ×°í ÀÌ·¯ÇÑ È¿°ú´Â ¼¼ Á¾·ùÀÇ HA Ç¥¸é ¸ðµÎ¿¡¼­ ÀϾÀ¸¸ç, POSÀÇ È°¼ºÁõ°¡´Â HA beads¿Í ¼Ò Ä¡¾Æ Ç¥¸é¿¡¼­¸¸ ³ªÅ¸³µ´Ù.
4. bLPO¿Í µÅÁöÀ§Àå mucinÀÇ È¥ÇÕ¹°À» HA Ç¥¸é¿¡ ºÎÂø½Ãų °æ¿ì, HA beads¿Í HA disc Ç¥¸é¿¡¼­ÀÇ peroxidase È°¼ºÀº Áõ°¡ÇÏ¿´´Ù.
5. bLPOÀÇ µÅÁöÀ§Àå mucin¿¡ ´ëÇÑ ºÎÂøģȭµµ´Â ¼Ò ¾ÇÇϼ± mucin¿¡ ºñÇØ ÄÇ´Ù.ÀÌ»óÀÇ °á°ú¸¦ Á¾ÇÕÇØ º¼ ¶§ µ¿¹°¼º mucinÀº ¿ë¾×»óÅÂ¿Í HA Ç¥¸é¿¡¼­ peroxidase È°¼º¿¡ ¿µÇâÀ» ¹ÌħÀ» ¾Ë ¼ö ÀÖÀ¸¸ç, µ¿¹°¼º mucinÀ» Æ÷ÇÔÇÏ°í Àִ Ÿ¾×´ëüÁ¦´Â ÀÎüŸ¾× ¹× Ÿ¾×´ëüÁ¦¿¡ ÀÖ´Â peroxidase È°¼º¿¡ ¿µÇâÀ» ¹ÌÄ¥ ¼ö ÀÖÀ» °ÍÀÌ´Ù.

Animal mucins have structural characteristics similar to human salivary mucins. Animal mucins have been regarded as suitable substances for saliva substitutes. Since animal mucin molecules in saliva substitutes and host-derived antimicrobial salivary molecules exist simultaneously in whole saliva and the pellicles of patients with dry mouth, interactions may occur between these molecules. The purpose of this study was to investigate the influence of animal mucins on peroxidase activity in solution and on the surface of hydroxyapatite (HA) surfaces. The effects of animal mucins on peroxidase activity were examined by incubating porcine gastric mucin (PGM) or bovine submaxillary mucin (BSM) with either bovine lactoperoxidase (bLPO) or saliva samples. For solid-phase assays, immobilized animal mucins or peroxidase on three different HA surfaces (HA beads, HA disc, and bovine tooth) were used. Peroxidase activity was determined with an NbsSCN assay.
The obtained results were as follows:
1. PGM enhanced the enzymatic activity of bLPO in solution phase. PGM did not affect the enzymatic activity of peroxidase in saliva sample (POS).
2. BSM did not affect the enzymatic activities of both bLPO and POS in solution phase.
3. HA-adsorbed PGM increased subsequent bLPO adsorption in all three HA phases. The activity of POS was increased on both the HA beads and bovine tooth.
4. The peroxidase activities on the HA beads and disc were increased when the HA surfaces were exposed to a mixture of bLPO and PGM.
5. The binding affinity of bLPO to PGM was greater than that of bLPO to BSM.
Collectively, our results suggest that animal mucins affects the enzymatic activity of peroxidase on the HA surfaces as well as in solution. Saliva substitutes containing animal mucins may affect the function of antimicrobial components in natural saliva and saliva substitutes.

Å°¿öµå

µÅÁö À§Àå mucin;¼Ò ¾ÇÇϼ± mucin;Ÿ¾×
Porcine gastric mucin;Bovine submaxillary mucin;Peroxidase;Saliva

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