Dr. Aaron  Montgomery  Dc image

Dr. Aaron Montgomery Dc

1450 Ne Village St
Fairview OR 97024
503 836-6497
Medical School: Other - Unknown
Accepts Medicare: No
Participates In eRX: No
Participates In PQRS: No
Participates In EHR: No
License #: 4015
NPI: 1528384625
Taxonomy Codes:

Request Appointment Information

Awards & Recognitions

About Us

Practice Philosophy


Medical Malpractice Cases

None Found

Medical Board Sanctions

None Found


None Found


Mechanism of Copper Uptake from Blood Plasma Ceruloplasmin by Mammalian Cells. - PloS one
Ceruloplasmin, the main copper binding protein in blood plasma, has been of particular interest for its role in efflux of iron from cells, but has additional functions. Here we tested the hypothesis that it releases its copper for cell uptake by interacting with a cell surface reductase and transporters, producing apoceruloplasmin. Uptake and transepithelial transport of copper from ceruloplasmin was demonstrated with mammary epithelial cell monolayers (PMC42) with tight junctions grown in bicameral chambers, and purified human (64)Cu-labeled ceruloplasmin secreted by HepG2 cells. Monolayers took up virtually all the (64)Cu over 16h and secreted half into the apical (milk) fluid. This was partly inhibited by Ag(I). The (64)Cu in ceruloplasmin purified from plasma of (64)Cu-injected mice accumulated linearly in mouse embryonic fibroblasts (MEFs) over 3-6h. Rates were somewhat higher in Ctr1+/+ versus Ctr1-/- cells, and 3-fold lower at 2 °C. The ceruloplasmin-derived (64)Cu could not be removed by extensive washing or trypsin treatment, and most was recovered in the cytosol. Actual cell copper (determined by furnace atomic absorption) increased markedly upon 24h exposure to holoceruloplasmin. This was accompanied by a conversion of holo to apoceruloplasmin in the culture medium and did not occur during incubation in the absence of cells. Four different endocytosis inhibitors failed to prevent 64Cu uptake from ceruloplasmin. High concentrations of non-radioactive Cu(II)- or Fe(III)-NTA (substrates for cell surface reductases), or Cu(I)-NTA (to compete for transporter uptake) almost eliminated uptake of (64)Cu from ceruloplasmin. MEFs had cell surface reductase activity and expressed Steap 2 (but not Steaps 3 and 4 or dCytB). However, six-day siRNA treatment was insufficient to reduce activity or uptake. We conclude that ceruloplasmin is a circulating copper transport protein that may interact with Steap2 on the cell surface, forming apoceruloplasmin, and Cu(I) that enters cells through CTR1 and an unknown copper uptake transporter.
Natural large-scale regeneration of rib cartilage in a mouse model. - Journal of bone and mineral research : the official journal of the American Society for Bone and Mineral Research
The clinical need for methods to repair and regenerate large cartilage and bone lesions persists. One way to make new headway is to study skeletal regeneration when it occurs naturally. Cartilage repair is typically slow and incomplete. However, an exception to this observation can be found in the costal cartilages, where complete repair has been reported in humans but the cellular and molecular mechanisms have not yet been characterized. In this study, we establish a novel animal model for cartilage repair using the mouse rib costal cartilage. We then use this model to test the hypothesis that the perichondrium, the dense connective tissue that surrounds the cartilage, is a tissue essential for repair. Our results show that full replacement of the resected cartilage occurs quickly (within 1 to 2 months) and properly differentiates but that repair occurs only in the presence of the perichondrium. We then provide evidence that the rib perichondrium contains a special niche that houses chondrogenic progenitors that possess qualities particularly suited for mediating repair. Label-retaining cells can be found within the perichondrium that can give rise to new chondrocytes. Furthermore, the perichondrium proliferates and thickens during the healing period and when ectopically placed can generate new cartilage. In conclusion, we have successfully established a model for hyaline cartilage repair in the mouse rib, which should be useful for gaining a more detailed understanding of cartilage regeneration and ultimately for developing methods to improve cartilage and bone repair in other parts of the skeleton.© 2014 American Society for Bone and Mineral Research.
MELD score as a predictor of early death in patients undergoing elective transjugular intrahepatic portosystemic shunt (TIPS) procedures. - Cardiovascular and interventional radiology
To Evaluate the MELD score as a predictor of 30-day mortality in patients undergoing elective TIPS procedures.This was a retrospective, IRB-approved study. The medical records of all patients who underwent a TIPS procedure between May 1, 1999 and June 1, 2003 in a single institution were reviewed. Patients who underwent elective TIPS were selected. Elective TIPS was performed in 119 patients with a mean age of 55.1 (+/- 9.6) years. The MELD and Child-Pugh scores before TIPS, etiology of cirrhosis, portosystemic gradients before and after TIPS, procedure time, and procedural complications were obtained from the medical records. The MELD and Child-Pugh scores before TIPS were compared between the survivor group (SG) and the early death (EDG) group. The early death rate was calculated for MELD score subgroups (1-10, 11-17, 18-24, and >24). Data were analyzed using the Fisher exact test, chi-square test and independent-sample t-test. A p value of less than 0.05 was considered significant.Technical success rate was 100%. The early death rate was 10.9% (13/119). The mean MELD scores before TIPS were 19.4 (+/- 5.9) (EDG) and 14 (+/- 4.2) (SG) (p = 0.025). The early death rate was highest in the pre-TIPS MELD > 24 subgroup. The Child-Pugh scores were 9.0 (+/- 1.6) (SG) and 9.8 +/- 1.06 (EDG) (p = 0.08). The mean portosystemic gradients before TIPS were 20.5 (+/- 7.7) mmHg (EDG) and 22.7 (+/- 7.3) (SG) (p > 1) and the mean portosystemic gradients after TIPS were 6.5 (+/- 3.5) (EDG) and 6.9 (+/- 2.4) (SG) (p > 1). The mean procedural times were 95.6 (+/- 8.4) min (EDG) and 89.2 (+/- 7.5) min (SG) (p > 1). No early death was attributed to a fatal complication during TIPS.The MELD score is useful in identifying patients at a higher risk of early death after an elective TIPS. On th basis of our results, we do not endorse elective TIPS in patients with MELD scores > 24.
Urine protein as a rapid screen for renal function in the ED: can it replace serum creatinine in selected patients? - Emergency radiology
Many radiology departments are unwilling to perform studies that require contrast administration to adult emergency department patients over the age of 35 without having a documented serum creatinine concentration of less than 2.0 mg/dl within a week of the study. Significant diagnostic delays may ensue waiting for this serum test. The present study was performed to determine whether a negative urine protein test, obtained by dip testing, will serve as a marker for a serum creatinine concentration below 2.0 mg/dl in emergency department patients who give no history of a disease which potentially could cause renal insufficiency. Emergency patients aged 35 years or more presenting to a university hospital who did not volunteer a history of hypertension, diabetes mellitus, multiple myeloma, or systemic lupus erythematosus in triage were enrolled. Only patients with a negative urine protein test whose serum creatinine was tested for other reasons were included. Of the 310 patients who had no protein in their urine and no history of disease which potentially could cause renal insufficiency, none had a serum creatinine concentration greater than 2.0 mg/dl (mean=0.82 mg/dl, SD 0.28). Ages ranged from 35 to 96 years (mean=59.7 years, SD=17.5). All patients would have qualified for a contrast load for contrast computed tomography studies or for intravenous pyelogram. In patients who do not have a known history of hypertension, multiple myeloma, systemic lupus erythematosus, diabetes mellitus, or specific renal disease, urine dip testing for protein in the emergency department may be a rapid and safe screen for imaging studies requiring contrast without having to await serum creatinine testing.
Albuterol helps resistance exercise attenuate unloading-induced knee extensor losses. - Aviation, space, and environmental medicine
While resistance exercise (REX) attenuates knee extensor (KE) mass and strength deficits during short-term unloading, additional treatments concurrently administered with REX are required to reduce the greater losses seen with longer periods of unloading.To determine whether albuterol helps REX attenuate unloading-induced KE losses, two groups of subjects strength trained their left thigh three times per week, and otherwise refrained from ambulatory and weight-bearing activity for 40 d while receiving a capsule dosing treatment (albuterol, placebo) with no crossover. A third group served as unloaded controls (CTRL). On days 0, 20, and 40, the following data were collected from the nonweight-bearing (left) thigh: cross-sectional area (CSA); integrated electromyography (IEMG); and concentric and eccentric KE strength measures. Thigh CSA was estimated using anthropometric methodology. IEMG was used to provide root mean square (RMS) values from submaximal (100 nm) and maximal isometric contractions. Concentric and eccentric strength were measured from eight-repetition unilateral leg press sets.Repeated-measures mixed-factorial 3 x 3 ANCOVAs with day 0 values as a covariate showed group by time interactions for concentric and eccentric total work (CTW, ETW). Tukey's post hoc test showed REX-albuterol evoked significant (p < 0.05) day 40 CTW and ETW gains vs. within-group day 0 and within-time REX-placebo and CTRL values. By days 20 and 40, CTRL subjects incurred significant decrements.Albuterol augmented the effects of REX to increase CTW and ETW. Research identifying possible mechanisms responsible for such changes, as well as the safety of REX-albuterol administration in other models, is warranted.

Map & Directions

1450 Ne Village St Fairview, OR 97024
View Directions In Google Maps

Nearby Doctors

1547 Ne Market Dr
Fairview, OR 97024
503 668-8000
1659 Ne Market Dr
Fairview, OR 97024
503 659-9100
20454 Ne Sandy Blvd Apt 38
Fairview, OR 97024
765 492-2825
3797 Ne Fairview Lake Way
Fairview, OR 97024
503 658-8751
22185 Ne Alton St
Fairview, OR 97024
503 742-2898
1606 Ne 223Rd Ave
Fairview, OR 97024
503 653-3608